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Molecular Organization of Various Collagen Fragments as Revealed by Atomic Force Microscopy and Diffusion‐Ordered NMR Spectroscopy
Author(s) -
Stötzel Sabine,
Schurink Marloes,
Wienk Hans,
Siebler Uschi,
BurgRoderfeld Monika,
Eckert Thomas,
Kulik Bianca,
Wechselberger Rainer,
Sewing Judith,
Steinmeyer Jürgen,
Oesser Steffen,
Boelens Rolf,
Siebert HansChristian
Publication year - 2012
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201200284
Subject(s) - hydrolysate , chemistry , atomic force microscopy , hydrolysis , enzymatic hydrolysis , biophysics , type i collagen , chemical engineering , biochemistry , nanotechnology , materials science , biology , engineering , endocrinology
Heterogeneous mixtures of collagen fragments can be used as nutrition supplement or as key ingredients for ointments with therapeutic relevance in wound healing. Some mixtures of collagen fragments are referred to as collagen hydrolysates owing to the production process with hydrolytic enzymes. Since the precise composition of collagen hydrolysates is generally unknown, it is of interest to analyze samples containing various collagen fragments with appropriate biophysical methods. Any product optimization without a profound knowledge concerning the size and the molecular weight distribution of its components is nearly impossible. It turned out that a combination of AFM methods with NMR techniques is exceptionally suited to examine the size range and the aggregation behavior of the collagen fragments in the hydrolysates of fish, jellyfish, chicken, porcine and bovine collagen. Supported by molecular modeling calculations, the AFM and NMR experiments provide a detailed knowledge about the composition of collagen hydrolysates and collagen ointments. Furthermore, the data allow a correlation between the size of the fragments and their potential bioactivity.