title: Structural alteration of collagen fibres--spectroscopic and mechanical studies.
abstract: Fourier Transform Near Infrared Raman Spectroscopy has been used to monitor the molecular changes of collagen in a tendon subjected to strain. In the Raman spectrum of the unstrained tendon, some protein bands, mainly assigned to collagen, can be observed: amide I (1666 cm-1) and III (1266 and 1248 cm-1) vibrational modes and skeletal (C-C) stretching vibrations (816 and 940 cm-1). The position of these bands is changing with the increasing strain values. It is concluded that elastin and non-helical domains of collagen are initially involved in the load transfer and triple helices of collagen are gradually joining this process.
authors.affiliation: Institute of Biomedical Engineering and Instrumentation, Wrocław University of Technology, Wrocław, Poland. marlena.gasior-glogowska@pwr.wroc.pl
authors.forename: Marlena
authors.initials: M
authors.lastname: Gąsior-Głogowska
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Komorowska
authors.forename: Jerzy
authors.initials: J
authors.lastname: Hanuza
authors.forename: Maciej
authors.initials: M
authors.lastname: Ptak
authors.forename: Magdalena
authors.initials: M
authors.lastname: Kobielarz
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena / Q000502:physiology; D055119:Elastic Modulus / Q000502:physiology; D024022:Fibrillar Collagens / Q000737:chemistry*; D013059:Spectrum Analysis, Raman / Q000379:methods*; D034421:Sus scrofa; D013623:Tail; D013710:Tendons / Q000502:physiology; D013997:Time Factors
chemical_list: D024022:Fibrillar Collagens