Nonlinear optical response of the collagen triple helix and second harmonic microscopy of collagen liquid crystals

A. Deniset-Besseau; P. De Sa Peixoto; J. Duboisset; C. Loison; F. Hache; E. Benichou; P.-F. Brevet; G. Mosser; M.-C. Schanne-Klein

doi:10.1117/12.840873

26 February 2010 Nonlinear optical response of the collagen triple helix and second harmonic microscopy of collagen liquid crystals

A. Deniset-Besseau, P. De Sa Peixoto, J. Duboisset, C. Loison, F. Hache, E. Benichou, P.-F. Brevet, G. Mosser, M.-C. Schanne-Klein

Author Affiliations +

Proceedings Volume 7569, Multiphoton Microscopy in the Biomedical Sciences X; 75691S (2010) https://doi.org/10.1117/12.840873
Event: SPIE BiOS, 2010, San Francisco, California, United States

Abstract

Collagen is characterized by triple helical domains and plays a central role in the formation of fibrillar and microfibrillar networks, basement membranes, as well as other structures of the connective tissue. Remarkably, fibrillar collagen exhibits efficient Second Harmonic Generation (SHG) and SHG microscopy proved to be a sensitive tool to score fibrotic pathologies. However, the nonlinear optical response of fibrillar collagen is not fully characterized yet and quantitative data are required to further process SHG images. We therefore performed Hyper-Rayleigh Scattering (HRS) experiments and measured a second order hyperpolarisability of 1.25 10^-27esu for rat-tail type I collagen. This value is surprisingly large considering that collagen presents no strong harmonophore in its amino-acid sequence. In order to get insight into the physical origin of this nonlinear process, we performed HRS measurements after denaturation of the collagen triple helix and for a collagen-like short model peptide [(Pro-Pro-Gly)₁₀]₃. It showed that the collagen large nonlinear response originates in the tight alignment of a large number of weakly efficient harmonophores, presumably the peptide bonds, resulting in a coherent amplification of the nonlinear signal along the triple helix. To illustrate this mechanism, we successfully recorded SHG images in collagen liquid solutions by achieving liquid crystalline ordering of the collagen triple helices.

Citation Download Citation

A. Deniset-Besseau, P. De Sa Peixoto, J. Duboisset, C. Loison, F. Hache, E. Benichou, P.-F. Brevet, G. Mosser, and M.-C. Schanne-Klein "Nonlinear optical response of the collagen triple helix and second harmonic microscopy of collagen liquid crystals", Proc. SPIE 7569, Multiphoton Microscopy in the Biomedical Sciences X, 75691S (26 February 2010); https://doi.org/10.1117/12.840873

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available

Members: $17.00

Non-members: $21.00 ADD TO CART

PROCEEDINGS
5 PAGES

DOWNLOAD PAPER SAVE TO MY LIBRARY

GET CITATION

RIGHTS & PERMISSIONS

Get copyright permission Get copyright permission on Copyright Marketplace

KEYWORDS

Collagen

Second-harmonic generation

Tissues

Microscopy

Liquid crystals

Liquids

Nonlinear optics

Show All Keywords

Keywords/Phrases

Search In:

Publication Years