Non-specific cleavage of collagen by proteinases in the presence of sodium dodecyl sulfate.
Proteolytic degradation of collagen normally requires specific collagenases of either mammalian or microbial origin. We have observed, among many detergents, a unique effect of sodium dodecyl (= lauryl) sulfate after preincubation of insoluble collagen (type I) with detergent. When treated fibrils were isolated and resuspended in detergent-free buffer, they were very sensitive to cleavage by non-specific proteases like trypsin, elastase, and subtilisin. We suggest that dodecyl sulfate causes a structural change in the collagen molecule which abrogates the resistance of collagen to most proteolytic enzymes. These observations may have implications for collagen and connective tissue research in general and especially to periodontal research. Lauryl sulfate (2-5%) is included in the majority of toothpaste formulations as a foaming agent, and our results again raise the question whether toothbrushing with lauryl sulfate may accelerate periodontal destruction by synergism with bacterial and host proteases. It may also bind to the collagen in exposed root surfaces and thus affect the stability of their hard tissues.
Bleeg
H S
HS
Department of Oral Biology, Royal Dental College, Arhus, Denmark.
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000378:metabolism*; D004549:Elastin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D051381:Rats; D012967:Sodium Dodecyl Sulfate / Q000009:adverse effects / Q000494:pharmacology*; D012995:Solubility; D013381:Subtilisins / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D012967:Sodium Dodecyl Sulfate; D003094:Collagen; D004549:Elastin; D010450:Endopeptidases; D013381:Subtilisins; D014357:Trypsin