Effect of monovalent anions on type I collagen fibrillogenesis in vitro.
The effect of a set of monovalent anions with different preferential binding to proteins (C1-, Br-, I-, SCN-) on the kinetics of type I collagen fibrillogenesis was studied. Evidences obtained from turbidity-time curves and the Arrenhius plot suggested the presence of a conformational change prior to fibril formation, also supported by previous data available in the literature. A model of the initial steps of collagen assembly was proposed that could explain the action of the monovalent anions studied and other cosolvents on fibrillogenesis. Analysis of fibril width and 1-anilinonaphthalene-8-sulfonic acid (ANS) binding to collagen pointed to the presence of a nucleation process within the lag time.
Delorenzi
N J
NJ
Departamento de Quimica-Fisica, Facultad de Cs. Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario. Argentina.
Sculsky
G
G
Gatti
C A
CA
D000838:Anions / Q000494:pharmacology*; D001965:Bromides / Q000494:pharmacology; D002712:Chlorides / Q000494:pharmacology; D003094:Collagen / Q000138:chemical synthesis / Q000502:physiology*; D007454:Iodides / Q000494:pharmacology; D009391:Nephelometry and Turbidimetry; D011487:Protein Conformation / Q000187:drug effects; D013861:Thiocyanates / Q000494:pharmacology; D013997:Time Factors
D000838:Anions; D001965:Bromides; D002712:Chlorides; D007454:Iodides; D013861:Thiocyanates; D003094:Collagen