ISSN:
0018-019X
Keywords:
Chemistry
;
Organic Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The influence of D-amino acid residues upon the conformative behaviour of collagen model peptides.(L-Pro-L-Pro-Gly)10 and (L-Pro-D(L)-Pro-Gly)10 with 10 percent D-Prolin residues have been synthesized by the Merrifield technique. Further Poly-(Gly-Pro-Pro) and Poly-(Ala-Gly-Pro) with various amounts of D-amino acid residues have been synthesized by polycondensation of the proper tripeptides. The conformational behaviour of all these polypeptides has been studied by measurements at varying temperatures of optical rotation, circular dichroism and molecular weight. The results show that limited amounts of D-amino acid residues do not impedecollagen-like triple helical conformations. The denaturation temperatures, however, are considerably lowered by D-amino acid residues. The implications of these findings for the understanding of the properties of partially racemized degraded gelatins with relatively low gel melting points are discussed.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/hlca.19760590449
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