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PubMed1980

Bradykinin analogs containing alpha-aminoisobutyric acid (Aib).

All seven possible bradykinin (BK) analogs contained Aib in place of proline have been synthesized by the solid phase method and assayed for in vitro myotropic activity on the guinea pig ileum and rat uterus, and in vivo on the rat blood pressure, both in intravenous and intra-aortic administration. [Aib(2,3)]-BK, [Aib(2,7)]-BK, and [Aib(2,3,7)]-BK had no in vivo or in vitro activities; [Aib(2)]-BK, [Aib(3)]-BK and [Aib(3,7)]-BK had moderate BK-like activities and a significantly increased resistance to pulmonary inactivation in the rat ([Aib(3,7)]-BK was totally resistant). [Aib(7)]-BK was found to be the most active position seven BK analog yet assayed on the rat blood pressure, and shows remarkably high ileum (4 times BK) and intravenous rat blood pressure (6 times BK) activity.

Aminoisobutyric Acids↗
PubMed1983

Stabilization of beta-turn conformations in enkephalins. alpha-Aminoisobutyric acid analogs.

Stereochemical constraints have been introduced into the enkephalin backbone by substituting alpha-aminoisobutyryl (Aib) residues at positions 2 and 3, instead of Gly. 1H n.m.r. studies of Tyr-Aib-Gly-Phe-Met-NH2, Tyr-Aib-Aib-Phe-Met-NH2 and Tyr-Gly-Aib-Phe-Met-NH2 demonstrate the occurrence of folded, intramolecularly hydrogen bonded structures in organic solvents. Similar conformations are also favoured in the corresponding t-butyloxycarbonyl protected tetrapeptides, which lack the Tyr residue. A beta-turn centred at positions 2 and 3 is proposed for the Aib2-Gly3 analog. In the Gly2-Aib3 analog, the beta-turn has Aib3-Phe4 as the corner residues. The Aib2-Aib3 analog adopts a consecutive beta-turn or 3(10) helical conformation. High in vivo biological activity is observed for the Aib2 and Aib2-Aib3 analogs, while the Aib3 peptide is significantly less active.

Aminoisobutyric Acids↗
PubMed1973

The rate equation and activation energies for the uptake of -aminoisobutyric acid by mouse brain slices.

1. The initial influx of the amino acid analogue AIB at medium concentrations of 0.05-20 mM into mouse cerebrum slices incubated at temperatures from 20 to 45 degrees C follows the rate law v = V(max)/(1 + K(t)/S)+k(u)S. The linear term k(u)S arises from an unsaturable process of concentrative uptake.2. At 37 degrees C the kinetic constants are K(t) = 1.12 mM; V(max) = 0.39 mumole AIB/g final wet wt. of slices. min; and k(u) = 0.054 mumole AIB/g final wet wt. of slices. mM-AIB. min.3. At infinitesmal substrate concentrations 13% of influx is via the unsaturable process. This rises to 73% for 20 mM substrate.4. K(t) is independent of temperature. The other constants increase rapidly with temperature. Arrhenius activation energies are 14.1 kcal/mole for V(max) and 17.4 kcal/mole for k(u).

Aminoisobutyric Acids↗
PubMed1986

Membrane channel forming polypeptides. Molecular conformation and mitochondrial uncoupling activity of antiamoebin, an alpha-aminoisobutyric acid containing peptide.

The conformations of the 16-residue fungal peptide antiamoebin I (Ac-Phe-Aib-Aib-Aib-D-Iva-Gly-Leu-Aib-Aib-Hyp-Gln-D-Iva-Hyp-Aib-Pro-P hol) have been investigated in dimethyl sulfoxide solution by one- and two-dimensional NMR techniques. A substantial number of resonances in the 270-MHz 1H NMR spectrum have been assigned. Intramolecularly hydrogen-bonded (solvent inaccessible) NH groups have been identified by determining solvent and temperature dependence of NH chemical shifts and rates of hydrogen-deuterium exchange. Ten backbone NH groups are inaccessible to solvent, while three NH groups assigned to the Phe(1), Aib(2), and Aib(8) residues are exposed to solvent. Interresidue nuclear Overhauser effects are consistent with psi values of approximately 120 +/- 30 degrees for Phe(1) and Leu(7). The NMR results, together with the stereochemical constraints imposed by the presence of alpha-aminoisobutyryl, isovalyl, prolyl, and 4-hydroxyprolyl residues, favor a highly ordered structure. Two backbone conformations consistent with the data are considered. Antiamoebin is shown to be an effective uncoupler of oxidative phosphorylation in rat liver mitochondria, providing evidence for its membrane-modifying activity.

Aminoisobutyric Acids↗
PubMed1982

Solution conformations of oligomers of alpha-aminoisobutyric acid.

The N-acetyl(Aib)nN'-methylamides (with n = 1, 2 and 3) and the N-acetyl-(Aib)3 methyl ester have been synthesized using an oxazolone procedure. An experimental conformational analysis of this series of oligomers has been carried out in water, DMSO-d6 and CDCl3 using n.m.r. techniques, and in chloroform using i.r. spectroscopy. Deuterium exchange rates of amide protons in DMSO-d6 and the rates of these proton chemical shifts with temperature in water, DMSO-d6 and CDCl3 indicate that the oligomeric N'-methylamides adopt conformations that have no hydrogen bonds when n = 1, one hydrogen bond when n = 2, and two hydrogen bonds when n = 3, and that Ac(Aib)3OMe has a conformation with one hydrogen bond. An analysis of the N-H stretching region of the i.r. spectra of these compounds in CHCl3 also suggests the existence of these conformational states. These data imply that the peptides adopt the 3(10)-helical and not the alpha-helical conformation in solution. This conclusion supports the hypothesis that the Aib residue has asymmetric geometry at the C alpha atom in solution, similar to that reported in the literature for the crystalline state.

Aminoisobutyric Acids↗
PubMed1993

Studies on the mechanism by which prolactin stimulates alpha-aminoisobutyric acid uptake into cultured mouse mammary tissues.

Studies were carried out to determine the possible roles of the polyamines, cyclic nucleotides, icosanoid products, and protein kinase C in the prolactin regulation of amino acid transport in cultured mammary gland explants derived from 12-14 day pregnant mice. Elevated cyclic AMP concentrations impaired the PRL stimulation of AIB transport. DBcAMP as well as the phosphodiesterase inhibitors theophylline and methyl isobutylxanthine, when added to the cultures, attenuated or abolished the PRL responses. 8-Bromo cyclic GMP elicited a modest stimulation of AIB transport. Ongoing polyamine synthesis appears to be necessary for PRL to effect a stimulation of AIB transport since methylglyoxal bis(guanyl hydrazone), an inhibitor of S-adenosyl methionine decarboxylase, abolishes the PRL response; specificity of this effect was established by its reversal with the addition of spermidine to the culture medium. Ongoing icosanoid product synthesis also appears to be required for the PRL stimulation of AIB transport since indomethacin abolishes the PRL response. Finally, the inhibition of the PRL response by the protein kinase C inhibitor H-7 suggests that the activation of kinase C activity may also be involved in the PRL stimulation of AIB transport.

1-Methyl-3-isobutylxanthine↗
PubMed1978

Role of Na+ in alpha-aminoisobutyric acid uptake by membrane vesicles from mouse fibroblasts transformed by simian virus 40.

The uptake of alpha-amino[(3)H]isobutyric acid (AIB) was studied in membrane vesicles from mouse fibroblasts transformed by simian virus 40 to examine the features of the Na(+)-stimulated and Na(+)-dependent AIB transport process. The simultaneous addition of NaCl and AIB to these vesicles produced a transient accumulation, or "overshoot," of amino acid 3-4 times the equilibrium value. Both the initial rate of uptake and the rate of fall of intravesicular AIB after maximal accumulation were sensitive to the temperature of incubation. The overshoot of AIB uptake was enhanced with Na(+) salts of highly permeant lipophilic anions, such as SCN(-) and NO(3) (-), and was decreased by the addition of SO(4) (2-), a relatively impermeant ion. Gramicidin D, which enhances the membrane conductance of Na(+) electrogenically, decreased the overshoot, while a potassium diffusion potential, induced by valinomycin (in K(+)-preloaded membrane vesicles), produced a Na(+)-dependent overshoot of AIB uptake. When vesicles were preincubated with both Na(+) and AIB, followed by the generation of an interior negative membrane potential (by the addition of SCN(-)), an overshoot of AIB uptake resulted. However, this did not occur in the absence of Na(+). It is concluded that, apart from its role in the generation of a transmembrane electrochemical potential, Na(+) is essential for the overshoot of AIB uptake.

Aminoisobutyric Acids↗
PubMedDate not supplied

Three-dimensional arrangement of sugar residues along a helical polypeptide backbone: synthesis of a new type of periodic glycopeptide by polymerization of a beta-O-glycosylated tripeptide containing alpha-aminoisobutyric acid.

A new type of glycopeptide having a periodic sequence of -[L-Glu(OMe)-Ser(beta-D-GlcNAc)-Aib]- was synthesized by polymerization of a glycosylated tripeptide with diphenylphosphoryl azide (DPPA) and active ester methods using H-L-Glu(OMe)-Ser[beta-D-GlcNAc(Ac)(3)]-Aib-OH (13) and H-L-Glu(OMe)-Ser[beta-D-GlcNAc(Ac)(3)]-Aib-ONp (15, Np = p-nitrophenyl) as the monomers, respectively. Number-average molecular weights were determined by size exclusion chromatography (SEC) and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry, those in the latter method were higher than those in the former one. CD and FT IR spectra of poly(13) and poly(15) indicated that they form right-handed helical conformations. Deacetylation of the acetylated glycopeptide was established without racemization using hydrazine/methanol. CD spectra of the deacetylated glycopeptides 16 (21 and 24 residues) in water showed negative Cotton effect at wavelength of 208 and 222 nm indicating an alpha-helical conformation, i.e., N-acetyl-D-glucosamine (GlcNAc) moieties were arranged spatially along the alpha-helical peptide keeping a specific distance and orientation in water. Addition of ethanol to aqueous solutions of the periodic glycopolymer 16 resulted in an increase in the alpha-helix content. Semiempirical molecular orbital calculation also supported the alpha-helical conformation of 16.

Aminoisobutyric Acids↗
PubMed1976

alpha-Aminoisobutyric acid transport in liver slices from rats fed low protein meals.

The effect of low protein intake on alpha-aminioisobutyric acid (AIB) transport has been examined in liver slices from meal-fed rats. Treatments (force-feeding casein or gelatin hydrolysates, glycine, or potassium chloride; injecting glucagon, or preincubating liver slices with cyclic AMP) which stimulated transport in control rat fed 3-hour meals containing 18% casein were less effective in rats fed 6% casein meals for 8 days. Responses of protein-depleted rats to glucagon or cyclic AMP had become essentially normal after they had consumed 18% casein meals for 2 days, whereas between 6 to 10 days were required for complete recovery of the response to casein hydrolysate. Stimulation of AIB transport by casein hydrolysate was also normal in depleted rats after they had consumed 40% casein meals for 2 days. Basal, non-stimulated transport of AIB was not significantly depressed in rats fed the low protein diet. Casein hydrolysate-induced increases in hepatic cyclic AMP concentrations were smaller in rats fed low protein meals. The results show that, although various stimuli of hepatic AIB transport become less effective in the protein-deprived rat, relatively rapid recovery of the response can occur upon refeeding adequate or high levels of protein.

Aminoisobutyric Acids↗
PubMed1988

Aqueous channels within apolar peptide aggregates: solvated helix of the alpha-aminoisobutyric acid (Aib)-containing peptide Boc-(Aib-Ala-Leu)3-Aib-OMe.2H2O.CH3OH in crystals.

Although the peptide Boc-Aib1-Ala2-Leu3-Aib4-Ala5-Leu6-Aib7-Ala8-L eu9-Aib10-OME [with a t-butoxycarbonyl (Boc) blocking group at the amino terminus, a methyl ester (OMe) at the carboxyl terminus, and four alpha-amino-isobutyric (Aib) residues] has a 3-fold repeat of residues, the helix formed by the peptide backbone is irregular. The carboxyl-terminal half assumes an alpha-helical form with torsion angles phi and psi of approximately -60 degrees and -45 degrees, respectively, whereas the amino-terminal half is distorted by an insertion of a water molecule between the amide nitrogen of Ala5 [N(5)] and the carbonyl oxygen of Ala2 [O(2)]. The water molecule W(1) acts as a bridge by forming hydrogen bonds N(5)...W(1) (2.93 A) and W(1)...O(2) (2.86 A). The distortion of the helix exposes the carbonyl oxygens of Aib1 and Aib4 to the outside environment, with the consequence that the helix assumes an amphiphilic character despite having all apolar residues. Neighboring helices in the crystal run in antiparallel directions. On one side of a helix there are only hydrophobic contacts with efficient interdigitation of leucine side chains with those from the neighboring helix. On the other side of the helix there are hydrogen bonds between protruding carbonyl oxygens and four water molecules that separate two neighboring helices. Along the helix axis the helices bind head-to-tail with a direct hydrogen bond N(2)...O(9) (3.00 A). Crystals grown from methanol/water solution are in space group P21 with a = 15.778 +/- 0.004 A, b = 11.228 +/- 0.002 A, c = 18.415 +/- 0.003 A, beta = 102.10 +/- 0.02 degrees, and two formula units per cell for C49H88N10O13.2H2O.CH3OH. The overall agreement factor R is 7.5% for 3394 reflections observed with intensities greater than 3 sigma (F), and the resolution is 0.90 A.

Aminoisobutyric Acids↗
PubMed1995

A nonhelical, multiple beta-turn conformation in a glycine-rich heptapeptide fragment of trichogin A IV containing a single central alpha-aminoisobutyric acid residue.

The conformational properties of the protected seven-residue C-terminal fragment of the lipopeptaibol antibiotic Trichogin A IV (Boc-Gly-Gly-Leu-Aib-Gly-Ile-Leu-OMe) has been examined in CDCl3 and (CD3)2SO by 1H-nmr. Evidence for a multiple beta-turn conformation [type I' at Gly(1)-Gly(2), type II at Leu(3)-Aib(4), and a type I' at Aib(4)-Gly(5)] suggests that Leu(3) has preferred an extended or semiextended conformation over a helical conformation in CDCl3. This structure is thus in contrast to earlier observations of seven-residue peptides containing a single central Aib preferring helical conformations in both solution and crystalline states. A structural transition to a frayed right-handed helix is observed in (CD3)2SO. These results suggest that nonhelical conformations may be important in Gly-rich peptides containing Aib. Further, the presence of amino acids with contradictory influences on backbone conformational freedom can lead to well-defined conformational transitions even in small peptides.

Amino Acid Sequence↗