Sivashankarappa Gurusiddappa

The Synthesis of Collagen Peptides and Characterization of Their Inhibitory Effects on the Collagen Binding Activities of Integrins α1β1 and α2β1

Integrins α1β1 and α2β1 are two major eukaryotic collagen receptors. Binding to collagen is primarily due to an A-domain located near the N-terminus of the alpha chains (α1A and α2A) [1,2] and requires the triple helical conformation of collagen and the presence of divalent cations such as Mg2+ or Mn2+. Here we report the identification of three high affinity binding sites in type I collagen for both A domains, two of which were further confirmed using synthetic collagen peptides that adopt triple-helical conformation.

Synthetic Peptides Mimic the Active Sites of Fibronectin Receptors from Gram-Positive Bacteria

Fibronectin is a large (~440 kDa) dimeric glycoprotein found in body fluids and the extracellular matrix of higher animals. This protein has been shown to affect numerous biological processes. Most of the biological functions of fibronectin appear to be related to its ability to serve as a substrate for the adhesion of eukaryotic cells (for review, see Hynes, 1985; Yamada, 1983). The cellular receptors that mediate cell adhesion to fibronectin are of the integrin type, a family of heterodimeric receptors consisting of an α-chain and a β-chain. Several integrins recognize structures in the fibronectin molecule. Thus, α5β1 and αvβ3 recognize and bind to a Arg-Gly-Asp (RGD) sequence located in the central part of fibronectin (Hynes, 1992).