Collagen fibril formation in the presence of alkyl sulfonate detergents.
The effects of sulfonate detergents on fibril formation by type I (rat tail tendon) collagen, untreated and pepsin-treated, were studied at two temperatures. Fluorescent probes and CD spectra were used to study possible conformational changes in the collagen. With untreated collagen, the rate of fibril formation was reduced by the presence of the detergents, particularly at the low temperature and when the detergent molecules had longer aliphatic chains. With pepsin-treated collagen, however, the rate was increased by the longer-chain detergent at the higher temperature. These observations are discussed in the light of present knowledge of the role of telopeptides and hydrophobic interactions in fibril formation.
Delorenzi
N J
NJ
Departamento de Química-Física, Facultad de Cs. Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Argentina.
Gatti
C A
CA
D000476:Alkanesulfonates / Q000737:chemistry / Q000494:pharmacology*; D000818:Animals; D002942:Circular Dichroism; D003094:Collagen / Q000502:physiology*; D003902:Detergents / Q000737:chemistry / Q000494:pharmacology*; D008433:Mathematics; D009994:Osmolar Concentration; D010434:Pepsin A / Q000494:pharmacology; D051381:Rats; D013050:Spectrometry, Fluorescence; D013696:Temperature
D000476:Alkanesulfonates; D003902:Detergents; D003094:Collagen; D010434:Pepsin A