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PubMed1981

[Ratio of the amounts of the mRNA poly A+/poly A- fractions in the myocardium and the life span of mRNA poly A+].

Two mRNA fractions, poly A+ and poly A- were found in the rat heart muscle. They comprise 30 and 70% of the entire mRNA, respectively. The ratio of the mRNA poly A+ to poly A- in the myocardium does not change in physiological aging. According to the kinetics of labelled precursor incorporation into mRNA, the life span of the main mass of mRNA poly A+ in the myocardium is about 4 hours.

Aging↗
PubMed1984

Preparation and biological properties of a highly active poly(G) X poly(C) inducer of interferon.

Experimental conditions necessary for the full expression of interferon-inducing activity by a complex of polyguanylic acid and polycytidylic acid included: (i) a sufficiently high molecular size of each homopolymer; (ii) annealing conditions which insured complete denaturation of polyguanylic acid self-structure; and (iii) the specific biological assay employed to assay interferon-inducing potency. The complex of polyguanylic acid and polycytidylic acid possessed several properties that suggested it may be an atypical polynucleotide interferon inducer. For instance, it was inactive in primary rabbit kidney cell cultures, usually exquisitely sensitive to polynucleotide interferon inducers, unless it was incubated on the cell cultures for prolonged times or in the presence of DEAE-dextran. Polyguanylic acid X polycytidylic acid could induce interferon in rabbits and mice but gave a more protracted response than did poly(I) X poly(C). Finally, poly(G) X poly(C) was, without any modification, resistant to degradation by serum nucleases.

Animals↗
PubMed2006

Poly(ADP-ribose) accumulation and enhancement of postischemic brain damage in 110-kDa poly(ADP-ribose) glycohydrolase null mice.

Poly(ADP-ribose) (PAR) is a polymer synthesized by poly(ADP-ribose) polymerases (PARPs) and metabolized into free adenosine diphosphate (ADP)-ribose units by poly(ADP-ribose) glycohydrolase (PARG). Perturbations in PAR synthesis have been shown to play a key role in brain disorders including postischemic brain damage. A single parg gene but two PARG isoforms (110 and 60 kDa) have been detected in mouse cells. Complete suppression of parg gene causes early embryonic lethality, whereas mice selectively lacking the 110 kDa PARG isoform (PARG(110)(-/-)) develop normally. We used PARG(110)(-/-) mice to evaluate the importance of PAR catabolism to postischemic brain damage. Poly(ADP-ribose) contents were higher in the brain tissue of PARG(110)(-/-) than PARG(110)(+/+) mice, both under basal conditions and after PARP activation. Distal middle cerebral artery occlusion caused higher increase of brain PAR levels and larger infarct volumes in PARG(110)(-/-) mice than in wild-type counterparts. Of note, the brain of PARG(110)(-/-) mice showed reduced heat-shock protein (HSP)-70 and increased cyclooxygenase-2 expression under both control and ischemic conditions. No differences were detected in brain expression/activation of procaspase-3, PARP-1, Akt, HSP-25 and interleukin-1beta. Our findings show that PAR accumulation worsens ischemic brain injury, and highlight the therapeutic potential of strategies capable of maintaining PAR homeostasis.

Adenosine Triphosphate↗
PubMed2005

Synthesis of poly(Pro-Hyp-Gly)(n) by direct poly-condensation of (Pro-Hyp-Gly)(n), where n=1, 5, and 10, and stability of the triple-helical structure.

Pro-Hyp-Gly is a characteristic amino acid sequence found in fibrous collagens, and (Pro-Hyp-Gly)(10), which has been widely used as a collagen-model peptide, forms a stable triple-helical structure. Here, we synthesized polypeptides consisting of the Pro-Hyp-Gly sequence by direct poly-condensation of (Pro-Hyp-Gly)(n), where n=1, 5, and 10, using 1-hydroxybenzotriazole and 1-ethyl-3-(3-dimethyl-aminopropyl)-carbodiimide hydrochloride in both phosphate buffer (pH=7.4) and dimethylsulfoxide (DMSO) solutions for 48 h at 20 degrees C. The reaction of (Pro-Hyp-Gly)(5) and (Pro-Hyp-Gly)(10) in DMSO successfully gave polypeptides with molecular weights over 10,000, whereas low molecular weight products were obtained by reaction in phosphate buffer (pH=7.4). In contrast, Pro-Hyp-Gly at a concentration of 50 mg/mL in phosphate buffer (pH=7.4) gave polypeptides with molecular weights over 10,000. The Fourier transform infrared (FTIR) and (1)H nuclear magnetic resonance (NMR) spectra of poly(Pro-Hyp-Gly)(10) revealed that the polymerization of (Pro-Hyp-Gly)(10) described in this report had no side reactions. Each polypeptide obtained shows a collagen-like triple-helical structure, and the triple-helical structures of poly(Pro-Hyp-Gly) and poly(Pro-Hyp-Gly)(10) were stable up to T=80 degrees C, which suggests that the high molecular weight promotes stability of the triple-helical structure, in addition to the high Hyp content. Furthermore, transmission electron microscopy (TEM) observations show that poly(Pro-Hyp-Gly)(10) aggregates to form nanofiber-like structures about 10 nm in width, which suggests that a Pro-Hyp-Gly repeating sequence contains enough information for triple-helix formation, and for subsequent nanofiber-like structure formation.

Amino Acid Sequence↗
PubMed1994

Hemocompatibility on graft copolymers composed of poly(2-methacryloyloxyethyl phosphorylcholine) side chain and poly(n-butyl methacrylate) backbone.

To improve the hemocompatibility on hydrophobic biomedical materials by a simple coating technique, graft copolymers composed of a hydrophilic side chain with phospholipid polar groups and a hydrophobic backbone were synthesized. The hydrophilic chain had phospholipid polar groups, poly[2-methacryloyloxyethyl phosphorylcholine (MPC)], and the hydrophobic backbone was poly[n-butyl methacrylate (BMA)]. Because the graft copolymers obtained could dissolve in ethanol, they could be used as a coating material. When the poly(MPC-graft-BMA) was coated onto a poly(BMA) membrane, the composition of the MPC units on the surface was maintained in the bulk graft copolymer even after immersion in water. Protein adsorption on the membrane coated with the graft copolymer from human plasma detected by a gold-colloid labeled immunoassay was drastically decreased compared with that on glass and the original membrane. Moreover, blood cell adhesion, activation, and aggregation on the membrane after contact with human citrated whole blood were suppressed by the coating of the graft copolymer. These results clearly show that the poly(MPC-graft-BMA) is a suitable material for improving hemocompatibility on the biomedical devices because of its protein adsorption and cell adhesion resistant properties.

Adsorption↗
PubMed1997

Effect of Solvent Quality on Reverse Micelle Formation and Water Solubilization by Poly(ethylene oxide)/Poly(propylene oxide) and Poly(ethylene oxide)/Poly(butylene oxide) Block Copolymers in Xylene

In addition to associating into ("normal") micelles in aqueous solutions, amphiphilic polyoxyalkylene block copolymers can form "reverse" micelles in organic solvents at sufficiently high copolymer concentrations (above the critical micellization concentration (CMC)) and in the presence of some water. The effects of solvent quality on the copolymer micellization in an organic solvent and on the solubilization of water in such systems are examined here for representative poly(ethylene oxide)-b-poly(propylene oxide)-b-poly(ethylene oxide) (PEO-PPO-PEO) and poly(butylene oxide)-b-poly(ethylene oxide) (PBO-PEO) copolymers. The solvent quality is modulated by the addition of cosolutes and by a change in the temperature. A number of notable observations are reported: Worsening the aqueous solvent conditions by the addition of NaCl (10 wt% with respect to water) almost doubles the CMC and the water solubilization capacity (WS) of a PEO-PPO-PEO copolymer in p-xylene. An increase in temperature makes water a worse and xylene a better solvent for the copolymer. The combined result of heating is an increase of the CMC for all three copolymers studied. This indicates that the formation of reverse micelles is exothermic, which is opposite to what has been observed for normal micelles. The effects of temperature on the water uptake are nonmonotonic: WS increased with temperature for a PEO-PPO-PEO copolymer with 40% PEO but decreased for a copolymer with 20% PEO. An increase in WS with temperature, followed by a decrease, with the maximum WS efficiency occurring at the "effective" cloud point of the copolymer is proposed in order to explain this observation. Copyright 1997 Academic Press. Copyright 1997Academic Press

Journal Article↗
PubMed2001

Adsorption of Poly(ethylene oxide)-Poly(lactide) Copolymers. Effects of Composition and Degradation.

The effect of chemical degradation of two diblock copolymers of poly(ethylene oxide) (E) and poly(lactide) (L), E(39)L(5) and E(39)L(20), on their adsorption at silica and methylated silica was investigated with in situ ellipsometry. Steric stablization of polystyrene dispersions was investigated in relation to degradation. Hydrolysis of the poly(lactide) block of the copolymers was followed at different temperatures and pH by using HPLC to measure the occurrence of lactic acid in solution. The block copolymers were quite stable in pH-unadjusted solution at low temperature, whereas degradation was facilitated by increasing temperature or lowering of the pH. Lower degradation rates of E(39)L(20) where observed at low temperature in comparison with those of E(39)L(5), whereas the degradation rates of the copolymers were quantitatively similar at high temperature. The adsorption of the copolymers at methylated silica substrates decreased with increasing degree of degradation due to the reduction in the ability of hydrophobic block to anchor the copolymer layer at the surface. At silica the adsorption initially increased with increasing degradation, particularly for E(39)L(20) due to deposition of aggregates onto the surface. After extensive degradation the adsorption of the copolymers at both silica and methylated silica resembled that of the corresponding poly(ethylene oxide) homopolymer. Overall, it was found that the eventual reduction in adsorption occurred at a lower degree of degradation for E(39)L(5) than for E(39)L(20). Mean-field calculations showed a reduced anchoring for the block copolymers with decreasing poly(lactide) block length at hydrophobic surfaces. In accordance with this finding, it was observed that polystyrene dispersions were stabilized by E(39)L(20) or E(39)L(5) in a way that depended on both the lactide block length and the degree of degradation. Upon degradation of the hydrophobic block, stabilization of the polystyrene dispersions was maintained initially, but eventually degradation resulted in destabilization. The average residual copolymer concentration required for stabilization of the polystyrene dispersions was much higher than the corresponding concentration of intact copolymer required for stabilization. Copyright 2001 Academic Press.

Journal Article↗
PubMed1998

In vitro biosynthesis of poly(3-hydroxybutyric acid) by using purified poly(hydroxyalkanoic acid) synthase of Chromatium vinosum.

Purified recombinant poly(hydroxyalkanoic acid) (PHA) synthase from Chromatium vinosum (PhaECCv) was used to examine in vitro the specific synthase activity, turnover of R-(-)-3-hydroxybutyryl coenzyme A (3HB-CoA) and poly(3-hydroxybutyric acid) formation under various conditions. The 3HB-CoA consumption was terminated by a reaction-dependent inactivation of the PHA synthase. Salts (MgCl2, CaCl2, NaCl), proteins (bovine serum albumin, lysozyme, phasine) or detergent (Tween 20) increased the 3HB-CoA turnover to 2.5-fold. Specific PHA synthase activity was only partially affected by the added components. In general, a higher concentration of salt often inhibited the activity of PhaECCv without affecting the yield according to 3HB-CoA turnover. NAD+ and NADP+ (2 mM) inhibited PhaECCv completely, whereas NADH and NADPH did not. Macroscopic poly(3HB) granules were formed in vitro if PhaECCv was incubated in the presence of sufficient amounts of 3HB-CoA and if MgCl2 was present. The form and size of the granules synthesized in vitro were affected by the concentration of the PHA synthase protein as well as by bovine serum albumin and the GA24 protein, a poly(3HB)-granule-associated protein of Alcaligenes eutrophus. Scanning electron micrographs from the synthesized granules were obtained. The granules consisted of poly(3HB) that had a molar mass in the range (1-2) x 10(6) g/mol.

3-Hydroxybutyric Acid↗
PubMed1975

[A calorimetric study of the triple helix formation: interaction of poly(C) - guanosine - protonated poly(C)].

The triple helix formation of poly(C) - guanosine - poly(C+) was investigated by the help of an LKB scanning micro-calorimeter. The existence of the triple helix could also be shown by recording the melting curves. The ultraviolet absorption at different wave lengths namely 275 nm, 260 nm, and 245 nm was plotted as a function of the temperature. Furthermore formation of the triple helix was shown by plotting the ultraviolet absorption at 245 nm during the increasing addition of guanosine solution to a fixed amount of poly(C) in the solution. Finally the formation of the triple helix was demonstrated by plotting the ultraviolet absorption at 245 nm of a certain mixture of the components while the pH value of the solution was continuously lowered. All these methods show that the monomer interacts with the polymer double helix to form a triple helix. The calorimetric measurements show that the reaction enthalpy is concentration dependent. Above a threshold concentration a rapid increase of the reaction enthalpy is observed. This increase occurs in a very narrow concentration interval. Above this interval a final value of the reaction enthalpy is reached. The amount of the reaction enthalpy for the interaction of guanosine with poly(C) - poly(C+) double helix is 5.5 Kcal (mol base triplet)-1.

Calorimetry↗
PubMed1988

Strand-specific transcription of the simple sequences poly[dG-dT):(dC-dA)] and poly[(dG-dA):(dC-dT)] in D. melanogaster embryos revealed by S1 nuclease treatment.

The transcription of different strands of the simple sequences poly[(dG-dT):(dC-dA)] and poly[(dG-dA):(dT-dC)] in Drosophila melanogaster embryos was studied. After selective labelling of one strand, the polymers were hybridized with immobilized RNA and hybrids were treated on filters with S1 nuclease. Appropriate control has shown that this treatment destroys sandwich-like complexes and leaves only true hybrids. Transcription of poly[(dG-dA):(dT-dC)] proved to be nearly symmetric, while poly(dG-dT) is transcribed 3-times more intensively than poly(dA-dC). Our approach allowed us to estimate the relative content of simple sequences in RNA.

Animals↗
PubMed1994

Formation and stability of acetaldehyde-induced crosslinks between poly-lysine and poly-deoxyguanosine.

The amino acid residue and nucleoside specificity of acetaldehyde-induced DNA-protein crosslinks (DPXLs) were studied using a modified filter binding assay. A 40% inhibition of acetaldehyde-induced pUC13 plasmid DNA-calf thymus histone crosslink formation was achieved by addition of 50 mM lysine (free base), while arginine was unable to affect crosslink formation at concentrations to 150 mM. Polymers (5-mers) of lysine (poly-lys5) were able to substitute for histones in acetaldehyde-induced plasmid crosslink formation, being equally effective at equimolar concentrations. Homopolymers (6-mers) of deoxyguanosine (poly-dG6) (but not deoxyadenosine, deoxycytidine or thymidine) served as an efficient substrate for acetaldehyde-induced DPXL formation, using either calf thymus histones or poly-lys5 as the protein source. Acetaldehyde-induced crosslinks between poly-dG6 and poly-lys5 were formed rapidly, but were unstable at 37 degrees C (a half-life or 1.5-2 h). Stability of these crosslinks was unaffected by pH at a range of 5.5-9.0 at 37 degrees C for 2 h. Results presented here suggest that unstable complexes of deoxyguanosine and lysine constitute a major portion of the DPXLs formed by acetaldehyde in vitro.

Acetaldehyde↗
PubMed1985

Reactivity and binding of benzo(a)pyrene diol epoxide to poly(dG-dC).(dG-dC) and poly(dG-m5dC).(dG-m5dC) in the B and Z forms.

The physical and covalent binding of the carcinogen benzo(a)pyrene-7,8-diol-9,10-oxide (BaPDE) to poly(dG-dC).(dG-dC) and poly(dG-m5dC).(dG-m5dC) in the B and Z forms were studied utilizing absorbance, fluorescence and linear dichroism techniques. In the case of poly(dG-dC).(dG-dC) the decrease in the covalent binding of BaPDE with increasing NaCl concentration (0.1-4 M) as the B form is transformed to the Z form is attributed to the effects of high ionic strengths on the reactivity and physical binding of BaPDE to the polynucleotides; these effects tend to obscure differences in reactivities with the B and Z forms of the nucleic acids. In the case of poly(dG-m5dC).(dG-m5dC) the B-to-Z transition is induced at low ionic strength (2 mM NaCl + 10 microM Co(NH3)6Cl3) and the covalent binding is found to be 2-3-times lower to the Z form than to the B form. Physical binding of BaPDE by intercalation, which precedes the covalent binding reaction, is significantly lower in the Z form than in the B form, thus accounting, in part, for the lower covalent binding. The linear dichroism characteristics of BaPDE covalently bound to the Z and B forms of poly(dG-m5dC).(dG-m5dC) are consistent with nonintercalative, probably external conformations of the aromatic pyrenyl residues.

7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide↗
PubMed2005

Reverse thermo-responsive poly(ethylene oxide) and poly(propylene oxide) multiblock copolymers.

Aiming at developing new reverse thermo-responsive polymers, poly(ethylene oxide)-poly(propylene oxide) multiblock copolymers were synthesized by covalently binding the two components using carbonyl chloride and diacyl chlorides as the coupling molecules. The appropriate selection of the various components allowed the generation of systems displaying much enhanced rheological properties. For example, 15 wt% aqueous solutions of an alternating poly(ether-carbonate) comprising PEO6000 and PPO3000 segments, achieved a viscosity of 140,000 Pas, while the commercially available Pluronic F127 displayed 5,000 Pas only. Furthermore, the structure of the chain extender played a key role in determining the sol-gel transition. While poly(ether-ester)s containing therephtaloyl (para) and isophtaloyl (metha) coupling units failed to gel at any concentration, a 15 wt% aqueous solution of the polymer chain-extended with phtaloyl chloride (ortho) gelled at 43 degrees C. The water solutions were also studied by dynamic light scattering and a clear influence of the PEO/PPO ratio on the aggregate size was observed. By incorporating short aliphatic oligoesters into the backbone, prior to the chain extension stage, reverse thermal gelation-displaying biodegradable poly(ether-ester-carbonate)s, were generated.

Absorbable Implants↗
PubMed2006

Biodegradable nanoparticles of amphiphilic triblock copolymers based on poly(3-hydroxybutyrate) and poly(ethylene glycol) as drug carriers.

New amorphous amphiphilic triblock copolymers of poly(3-hydroxybutyrate)-poly(ethylene glycol)-poly(3-hydroxybutyrate) (PHB-PEG-PHB) were synthesized using the ring-opening copolymerization of beta-butyrolactone monomer. They were characterized by fluorescence, SEM and (1)H NMR. These triblock copolymers can form biodegradable nanoparticles with core-shell structure in aqueous solution. Comparing to the poly(ethylene oxide)-PHB-poly(ethylene oxide) (PEO-PHB-PEO) copolymers, these nanoparticles exhibited much smaller critical micelle concentrations and better drug loading properties, which indicated that the nanoparticles were very suitable for delivery carriers of hydrophobic drugs. The drug release profile monitored by fluorescence showed that the release of pyrene from the PHB-PEG-PHB nanoparticles exhibited the second-order exponential decay behavior. The initial biodegradation rate of the PHB-PEG-PHB nanoparticles was related to the enzyme amount, the initial concentrations of nanoparticle dispersions and the PHB block length. The biodegraded products detected by (1)H NMR contained 3HB monomer, dimer and minor trimer, which were safe to the body.

Absorbable Implants↗
PubMed2005

Poly(ethylene oxide)-modified poly(epsilon-caprolactone) nanoparticles for targeted delivery of tamoxifen in breast cancer.

This study was carried out to evaluate and compare the biodistribution profile of tamoxifen when administered intravenously (i.v.) as a simple solution or when encapsulated in polymeric nanoparticulate formulations, with or without surface-stabilizing agents. Tamoxifen-loaded, poly(ethylene oxide)-modified poly(epsilon-caprolactone) (PEO-PCL) nanoparticles were prepared by solvent displacement process that allowed in situ surface modification via physical adsorption of poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide) (PEO-PPO-PEO) triblock polymeric stabilizer (Pluronic). The nanoparticles were characterized for particle size and surface charge. Presence of PEO chains on nanoparticle surface was ascertained by electron spectroscopy for chemical analysis (ESCA). In vivo biodistribution studies were carried out in Nu/Nu athymic mice bearing a human breast carcinoma xenograft, MDA-MB-231 using tritiated [(3)H]-tamoxifen as radio-marker for quantification. PEO-PCL nanoparticles with an average diameter of 150-250 nm, having a smooth spherical shape, and a positive surface charge were obtained with the formulation procedure. About 90% drug encapsulation efficiency was achieved when tamoxifen was loaded at 10% by weight of the polymer. Aqueous wettability, suspendability, and ESCA results showed surface hydrophilization of the PCL nanoparticles by the Pluronics. The primary site of accumulation for the drug-loaded nanoparticles after i.v. administration was the liver, though up to 26% of the total activity could be recovered in tumor at 6h post-injection for PEO-modified nanoparticles. PEO-PCL nanoparticles exhibited significantly increased level of accumulation of the drug within tumor with time as well as extended their presence in the systemic circulation than the controls (unmodified nanoparticles or the solution form). Pluronic surfactants (F-68 and F-108) presented simple means for efficient surface modification and stabilization of PCL nanoparticles to achieve preferential tumor-targeting and a circulating drug reservoir for tamoxifen.

Animals↗
PubMed2003

Poly(ethylene glycol)-grafted poly(3-hydroxyundecenoate) networks for enhanced blood compatibility.

Poly(ethylene glycol)-grafted poly(3-hydroxyundecenoate) (PEG-g-PHU) networks were prepared by irradiating homogeneous solutions of poly(3-hydroxyundecenoate) (PHU) and the monoacrylate of poly(ethylene glycol) (PEG) with UV light. The resulting polymer networks were characterized by measuring the water contact angle, water uptake, and mechanical properties and by performing attenuated total reflectance infrared spectroscopy and scanning electron microscopy. These measurements showed that the PEG chains were present in polymer networks. Adsorption of blood proteins and platelets on cross-linked PHU (CLPHU) and PEG-g-PHU were examined using poly(L-lactide) (PLLA) surfaces as control. Blood proteins and platelets had significantly lower tendency of adhesion to surfaces composed of CLPHU and PEG-g-PHU networks than to PLLA. Blood compatibility of polymer networks increased as the fraction of grafted PEG increased. The results of this study suggest that PEG-g-PHU networks might be useful for blood-compatible biomedical applications.

Adsorption↗
PubMed1996

Elastase-induced hydrolysis of synthetic solid substrates: poly(ester-urea-urethane) and poly(ether-urea-urethane).

Human neutrophil elastase (HNE) and porcine pancreatic elastase (PPE) were incubated with two radiolabelled model poly(urethane), a poly(ester-urea-urethane) containing [14C]toluene diisocyanate ([14C]TDI), poly(caprolactone)(PCL) and ethylenediamine (ED), and a poly(ether-urea-urethane) containing [14C]TDI, poly(tetramethylene oxide) (PTMO) and ED. Ten-fold more radioactive carbon was released when PPE was incubated with [14C]TDI/PCL/ED than when HNE was used. The PPE-induced radioactive carbon release was significantly reduced by a specific elastase inhibitor. Ten-fold less radioactive carbon was released when [14C]TDI/PTMO/ED was incubated with PPE as compared to [14C]TDI/PCL/ED. Since neutrophils, which contain elastolytic activity, are present during the inflammatory response, the stability of biomaterials used in implanted devices may be affected.

Animals↗
PubMed2002

The effect of poly(ethylene glycol)-poly(D,L-lactic acid) diblock copolymers on peptide acylation.

The combination of poly(ethylene glycol) (PEG) with a biodegradable poly(ester), such as poly(D,L-lactic acid) (PLA), is an approach that has been successfully used for the stabilization of proteins and peptides in several biodegradable delivery devices. The acylation of peptides inside degrading PLA microspheres has been described only recently as another instability mechanism related to the accumulation of polymer degradation products inside eroding PLA. We investigated whether the block copolymerization of PLA with PEG reduces peptide acylation inside degrading microspheres. Diblock copolymers consisting of poly(D,L-lactic acid) covalently bound to poly(ethylene glycol)-monomethyl ether (Me.PEG-PLA) were used for these investigations. Human atrial natriuretic peptide (ANP) was incorporated into microspheres manufactured from Me.PEG5-PLA45, a diblock copolymer with an overall PEG content of 10%. Peptide integrity inside the microspheres was monitored by HPLC-MS analysis during 4 weeks of microsphere degradation in isotonic phosphate buffer (pH 7.4) at 37 degrees C. Inside the degrading Me.PEG5-PLA45 microspheres, acylation products as well as an oxidation product of ANP were formed. The results demonstrate that the combination of PEG with PLA does not necessarily display a favorable effect concerning peptide acylation inside degrading polymer microspheres. However, they also suggested that the acylation reaction is mainly driven by the formation and accumulation of polymer degradation products inside the degrading microspheres.

Acylation↗