title: Imino acids and collagen triple helix stability: characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats.
abstract: The analysis of factors contributing to the stability of proteins is a subject of intense debate. Particularly challenging is the study of structural proteins, since their function is their structure. Among these is collagen, the key structural component of bones, skin, cartilage, tendons, and other connecting tissues. It is well established that the collagen triple helix is characterized by the presence of hydroxyproline, whose content modulates triple helix thermal stability according to the requirement of the host organism. Because of the complexity and the fibrous nature of collagen, data on the stability and structure of this protein have been mainly obtained by the use of collagen-like polypeptides. On the basis of CD characterization of collagen-like polypeptides we here show that the presence of Hyp at the X position of repeating triplets Hyp-Hyp-Gly stabilizes the triple helix significantly. This extra-stabilization has been ascribed, by using molecular modeling, to the formation of a hydrogen bond between Hyp residues belonging to the X and the Y positions of adjacent chains. This communication also provides a comprehensive interpretation of the ensemble of available data on polypeptides containing proline derivatives.
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR; Dipartimento di Chimica Biologica, Università degli Studi di Napoli Federico II, Centro interuniversitario di ricerca sui Peptidi bioattivi (C.I.R.P.E.B.), Via Mezzocannone 6, I-80134 Naples, Italy.
authors.forename: Rita
authors.initials: R
authors.lastname: Berisio
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Granata
authors.forename: Luigi
authors.initials: L
authors.lastname: Vitagliano
authors.forename: Adriana
authors.initials: A
authors.lastname: Zagari
mesh_terms: D003094:Collagen / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry*; D006909:Hydroxyproline / Q000737:chemistry*; D007098:Imino Acids / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D012091:Repetitive Sequences, Nucleic Acid
chemical_list: D007098:Imino Acids; D010455:Peptides; D003094:Collagen; D006909:Hydroxyproline; D005998:Glycine