Abstract
Abnormal formation and organization of collagen network is commonly observed in many organ pathologies, but analytical techniques able to reveal the collagen biodistribution are still lacking. In this study, Fourier-transform infrared (FTIR) spectroscopy has been used to analyze type I, III, IV, V, and VI collagens, the most important compounds of connective tissues. A robust classification of 30 FTIR spectra per collagen type could be obtained by using a combination of four spectral intervals [ν(C=O) absorption of amide I (1,700–1,600 cm−1), δ(CH2), and δ(CH3) absorptions (1,480–1,350 cm−1), ν(C–N), and δ(N–H) absorptions of amide III (1,300–1,180 cm−1), and ν(C–O) and ν(C–O–C) absorptions of carbohydrate moieties (1,100–1,005 cm−1)]. Then, a submolecular justification of this classification model was sought using a curve fitting analysis of the four spectral intervals. Results demonstrated that every spectral interval used for the classification contained highly discriminant absorption bands between all collagen types (multivariate analysis of variance, p < 0.01; Dunnett's T3 post hoc test, p < 0.05). All conditions seem thus joined to make FTIR spectroscopy and imaging major tools for implementing innovative methods in the field of molecular histology, which would be very helpful for the diagnosis of a wide range of pathologies.
Similar content being viewed by others
Abbreviations
- FTIR:
-
Fourier-transform infrared
- RMSE:
-
Root mean square error
References
Brodsky B, Ramshaw JA (1997) Matrix Biol 15:545–554
Lampe AK, Bushby KM (2005) J Med Genet 42:673–685
Passerini L, Bernasconi P, Baggi F, Confalonieri P, Cozzi F, Cornelio F, Mantegazza R (2002) Neuromuscul Disord 12:828–835
Tsukada S, Parsons CJ, Rippe RA (2006) Clin Chim Acta 364:33–60
Stempien-Otero A, Plawman A, Meznarich J, Dyamenahalli T, Otsuka G, Dichek DA (2006) J Biol Chem 281:15345–15351
Whitelaw SE (2003) Pediatr Nurs 29:423–426
Sifre L, Berge P, Engel E, Martin JF, Bonny JM, Listrat A, Taylor R, Culioli J (2005) J Agric Food Chem 53:8390–8399
Listrat A, Lethias C, Hocquette JF, Renand G, Menissier F, Geay Y, Picard B (2000) Histochem J 32:349–356
Passerieux E, Rossignol R, Chopard A, Carnino A, Marini JF, Letellier T, Delage JP (2006) J Struct Biol 154:206–216
Petibois C, Deleris G (2006) Trends Biotechnol 24:455–462
Cohenford MA, Rigas B (1998) Proc Natl Acad Sci USA 95:15327–15332
Yano K, Ohoshima S, Gotou Y, Kumaido K, Moriguchi T, Katayama H (2000) Anal Biochem 287:218–225
Wehbe K, Pinneau R, Moenner M, Deleris G, Petibois C (2008) Anal Bioanal Chem 392:129–135
Levine SM, Wetzel DL (1998) Free Radic Biol Med 25:33–41
Bi X, Li G, Doty SB, Camacho NP (2005) Osteoarthritis Cartilage 13:1050–1058
Petibois C, Deleris G, Piccinini M, Cestelli Guidi M, Marcelli A (2009) Nat Photonics 3:179
Petibois C, Gouspillou G, Wehbe K, Delage JP, Deleris G (2006) Anal Bioanal Chem 386:1961–1966
Boskey AL, Gadaleta S, Gundberg C, Doty SB, Ducy P, Karsenty G (1998) Bone 23:187–196
Crupi V, De Domenico D, Interdonato S, Majolino D, Maisano G, Migliardo P, Venuti V (2001) J Mol Struct 563–4:115–118
Ward JH (1963) J Am Stat Assoc 58:236–244
Petibois C, Cazorla G, Gin H, Deleris G (2001) J Lab Clin Med 137:184–190
Haris PI, Severcan F (2001) J Mol Catal B: Enzym 7:207–221
Camacho NP, West P, Torzilli PA, Mendelsohn R (2001) Biopolymers 62:1–8
Liu KZ, Dixon IM, Mantsch HH (1999) Cardiovasc Pathol 8:41–47
Goormaghtigh E, Ruysschaert JM, Raussens V (2006) Biophys J 90:2946–2957
Fabian H, Naumann D (2004) Methods 34:28–40
Troullier A (2000) Nat Struct Biol 7:78–86
Haris PI, Servecan F (1999) J Mol Catal B: Enzym 6:207–221
Lee SM, Lin SY, Liang RC (1995) Artif Cells Blood Substit Immobil Biotechnol 23:193–205
Lasch P, Haensch W, Naumann D, Diem M (2004) Biochim Biophys Acta 1688:176–186
Kalluri R (2003) Nat Rev Cancer 3:422–433
Birk DE (2001) Micron 32:223–237
Acknowledgment
The authors are indebted to the “Association Française contre les Myopathies” (AFM) for their financial support.
Author information
Authors and Affiliations
Corresponding author
Electronic supplementary material
Below is the link to the electronic supplementary material.
ESM Table S1–S4
Table S1: Secondary structure parameters of collagen types. All values are spectral integration results obtained from amides I and II (1,720–1,480 cm−1) spectral interval curve fitting. a = significantly different from type I collagen; b = significantly different from type III collagen; c = significantly different from type IV collagen; d = significantly different from type V collagen; e = significantly different from type VI collagen. Table S2: IR absorption bands obtained from the 1,500–1,300 cm−1 spectral interval curve fitting. See supplementary data 1 for details on statistics. Table S3: IR absorption bands obtained from the 1,350–1,150 cm−1 spectral interval curve fitting. See Table S1 for details on statistics. Table S4: IR absorption bands obtained from the 1,130–950 cm−1 spectral interval curve fitting. See Table S1 for details on statistics. (PDF 58 kb)
Rights and permissions
About this article
Cite this article
Belbachir, K., Noreen, R., Gouspillou, G. et al. Collagen types analysis and differentiation by FTIR spectroscopy. Anal Bioanal Chem 395, 829–837 (2009). https://doi.org/10.1007/s00216-009-3019-y
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00216-009-3019-y