Analysis of type I and IV collagens by FT-IR spectroscopy and imaging for a molecular investigation of skeletal muscle connective tissue.
Many muscular diseases result from abnormal organization of connective tissue and/or collagen network formation. Only a few molecular imaging techniques are able to analyze this collagen network by differentiating collagen types. In this study, FT-IR spectroscopy was used to analyze type I and IV collagens, the most important compounds of which are perimysium and endomysium, respectively. Secondary structure of collagen types was determined by curve-fitting the 1,700-1,480 cm(-1) spectral interval. Type I collagen could be differentiated from type IV by its higher amounts of triple helix and alpha-helix, but lower amounts of beta-sheets (P < 0.01). FT-IR imaging was then used to determine structural features of perimysium and endomysium collagen network in bovine Flexor carpi radialis muscle. Secondary structure of proteins contained in perimysium and endomysium was found to be very close to type I and IV collagens, respectively. FT-IR spectroscopy and imaging are thus analytical tools that might be used for investigating biodistribution and assembly of collagen types in connective tissues.
Petibois
Cyril
C
CNRS UMR 5084, CNAB, Bio-Organic Chemistry Group, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux Cedex, France. cyril.petibois@u-bordeaux2.fr
Gouspillou
Gilles
G
Wehbe
Katia
K
Delage
Jean-Paul
JP
Déléris
Gérard
G
D020816:Amino Acid Motifs; D000818:Animals; D002417:Cattle; D024042:Collagen Type I / Q000032:analysis* / Q000737:chemistry; D024141:Collagen Type IV / Q000032:analysis* / Q000737:chemistry; D003238:Connective Tissue / Q000737:chemistry*; D007091:Image Processing, Computer-Assisted / Q000379:methods*; D008297:Male; D018482:Muscle, Skeletal / Q000737:chemistry*; D051381:Rats; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
D024042:Collagen Type I; D024141:Collagen Type IV