Search PubMed⌕ Search

Biomedical subjects

R B Rao

Publications and source records attributed to R B Rao.

27 records · Page 2Linked to original sources
PubMed1995

Contrasting solution conformations of peptides containing alpha,alpha-dialkylated residues with linear and cyclic side chains.

The conformational properties of alpha,alpha-dialkylated amino acid residues possessing acyclic (diethylglycine, Deg; di-n-propylglycine, Dpg; di-n-butylglycine, Dbg) and cyclic (1-aminocycloalkane-1-carboxylic acid, Acnc) side chains have been compared in solution. The five peptides studied by nmr and CD spectroscopy are Boc-Ala-Xxx-Ala-OMe, where Xxx = Deg (I), Dpg (II), Dbg (III), Ac6c (IV), and Ac7c (V). Delineation of solvent-shielded NH groups have been achieved by solvent and temperature dependence of NH chemical shifts in CDCl3 and (CD3)2SO and by paramagnetic radical induced line broadening in peptide III. In the Dxg peptides the order of solvent exposure of NH groups is Ala(1) > Ala(3) > Dxg(2), whereas in the Acnc peptides the order of solvent exposure of NH groups is Ala(1) > Acnc(2) > Ala(3). The nmr results suggest that Acnc peptides adopt folded beta-turn conformations with Ala(1) and Acnc(2) occupying i + 1 and i + 2 positions. In contrast, the Dxg peptides favor extended C5 conformations. The conformational differences in the two series are clearly borne out in CD studies. The solution conformations of peptides I-III are distinctly different from the beta-turn structure observed in crystals. Low temperature nmr spectra recorded immediately after dissolution of crystals of peptide II provide evidence for a structural transition. Introduction of an additional hydrogen-bonding function in Boc-Ala-Dpg-Ala-NHMe (VI) results in a stabilization of a consecutive beta-turn or incipient 3(10)-helix in solution.

Alkylation↗
PubMed1994

Coexistence of folded and extended conformations of a tripeptide containing alpha, alpha -di-n-propylglycine in crystals.

The crystal structure of the tripeptide Boc-Leu-Dpg-Val-OMe (Dpg, alpha, alpha -di-n-propylglycine) reveals the coexistence of two distinct backbone conformations. In molecule A the Dpg residue adopts a fully extended conformation (phi = 76.0 degrees, psi = 180.0 degrees) while in molecule B a left handed helical conformation (phi = 62.8 degrees, psi = 39.6 degrees) is observed. Molecule B adopts a folded structure corresponding to a highly distorted Type II beta-turn conformation, which lacks an intramolecular 4 -> 1 hydrogen bond. In contrast, molecule A has an open, extended conformation. The results demonstrate that both fully extended and helical conformations are energetically accessible to the Dpg residue.

Models, Molecular↗
PubMed1991

Stereochemistry of peptides containing 1-aminocycloheptane-1-carboxylic acid (Ac7c).

The crystal structures of four peptides incorporating 1-aminocycloheptane-1-carboxylic acid (Ac7c) are described. Boc-Aib-Ac7c-NHMe and Boc-Pro-Ac7c-Ala-OMe adopt beta-turn conformations stabilized by an intramolecular 4----1 hydrogen bond, the former folding into a type-I/III beta-turn and the latter into a type-II beta-turn. In the dipeptide esters, Boc-Aib-Ac7c-OMe and Boc-Pro-Ac7c-OMe, the Ac7c and Aib residues adopt helical conformations, while the Pro residue remains semi-extended in both the molecules of Boc-Pro-Ac7c-OMe found in the asymmetric unit. The cycloheptane ring of Ac7c residues adopts a twist-chair conformation in all the peptides studied. 1H-NMR studies in CDCl3 and (CD3)2SO and IR studies in CDCl3 suggest that Boc-Aib-Ac7c-NHMe and Boc-Pro-Ac7c-Ala-OMe maintain the beta-turn conformations in solution.

Amino Acid Sequence↗
PubMed1984

Calcium and phosphorus intakes, balances, and blood levels of adults consuming self-selected diets.

Metabolic calcium and phosphorus balances, blood calcium and phosphorus levels, and alkaline phosphatase activity of 34 men and women, 20 to 53 yr of age, were determined each season during 1 yr while consuming customary diets. Dietary records were maintained 365 days. Analysis of variance indicated that serum Ca, P, and alkaline phosphatase levels were affected by season (p less than 0.0001), whereas calcium or phosphorus intakes were not. Calcium and phosphorus intakes of the men (1075 and 1533 mg, respectively) were higher (p less than 0.01) than of the women (695 and 1095 mg, respectively), but balances were not statistically different between them. Daily calcium balances for the men and women for the year were -81 and -85 mg, respectively; daily phosphorus balances were -239 and -130 mg, respectively. Stepwise regression analysis indicated that dietary calcium and protein were significantly associated with calcium and phosphorus balances, but in opposite directions, and only in women over 35 yr of age.

Adult↗
PubMed1984

Magnesium intakes, balances, and blood levels of adults consuming self-selected diets.

Magnesium balances and plasma and blood cell concentrations were determined in 34 men and women, 20 to 53 yr of age, during each season for 1 yr while they were consuming their customary diets. Dietary records were maintained 365 days. Analysis of variance indicated no seasonal variation in intake or balance. Blood cell magnesium correlated with magnesium intake (r2 = 0.203; p less than 0.04). Daily magnesium intakes of the men (323 mg) were significantly higher (p less than 0.01) than of the women (234 mg), and reflected greater calorie consumption for their greater body weights. Daily magnesium balances for the men and women were -32 and -25 mg, respectively. Multiple regression analysis showed that magnesium balance was associated not only with magnesium intake but also with the intake of other nutrients such as fiber, protein, calcium, and phosphorus. Moreover, the effect of these nutrients on magnesium balance varied with age and sex.

Adult↗
PubMedDate not supplied

Conformationally restricted formyl methionyl tripeptide chemoattractants: a three-dimensional structure-activity study of analogs incorporating a C alpha,alpha-dialkylated glycine at position 2.

The conformationally restricted CHO-L-Met-Xxx-L-Phe-OY (where Xxx = Aib, Ac3c, Ac5c, Ac6c, and Ac7c; Y = H, Me) tripeptides, analogs of the chemoattractant CHO-L-Met-L-Leu-L-Phe-OH, have been synthesized in solution by classical methods and fully characterized. Compounds were compared to determine the combined effect of backbone conformational preferences and side-chain bulkiness on the relation of three-dimensional structure to biological activity. Each peptide was tested for its ability to induce granule enzyme secretion from rabbit peritoneal polymorphonuclear leukocytes. In parallel, a conformational analysis on the CHO-blocked peptide and their tertbutyloxycarbonylated synthetic precursors was performed in the crystal state and in solution using X-ray diffraction, infrared absorption, and 1H nuclear magnetic resonance. The biological and conformational data are discussed in relation to the proposed model of the chemotactic peptide receptor of rabbit neutrophils.

Alkylation↗