Measurement of the quadratic hyperpolarizability of the collagen triple helix and application to second harmonic imaging of natural and biomimetic collagenous tissues

A. Deniset-Besseau; M. Strupler; J. Duboisset; P. De Sa Peixoto; E. Benichou; C. Fligny; P.-L. Tharaux; G. Mosser; P.-F. Brevet; M.-C. Schanne-Klein

doi:10.1117/12.829882

24 September 2009 Measurement of the quadratic hyperpolarizability of the collagen triple helix and application to second harmonic imaging of natural and biomimetic collagenous tissues

A. Deniset-Besseau, M. Strupler, J. Duboisset, P. De Sa Peixoto, E. Benichou, C. Fligny, P.-L. Tharaux, G. Mosser, P.-F. Brevet, M.-C. Schanne-Klein

Author Affiliations +

Proceedings Volume 7487, Optical Materials in Defence Systems Technology VI; 74870E (2009) https://doi.org/10.1117/12.829882
Event: SPIE Security + Defence, 2009, Berlin, Germany

Abstract

Collagen is a major protein of the extracellular matrix that is characterized by triple helical domains. It 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) so that SHG microscopy proved to be a sensitive tool to probe the three-dimensional architecture of fibrillar collagen and to assess the progression of fibrotic pathologies. We obtained sensitive and reproducible measurements of the fibrosis extent, but we needed quantitative data at the molecular level to further process SHG images. We therefore performed Hyper- Rayleigh Scattering (HRS) experiments and measured a second order hyperpolarisability of 1.25 10^-27 esu for rat-tail type I collagen. This value is surprisingly large considering that collagen presents no strong harmonophore in its aminoacid 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 collagenous biomimetic matrices.

Citation Download Citation

A. Deniset-Besseau, M. Strupler, J. Duboisset, P. De Sa Peixoto, E. Benichou, C. Fligny, P.-L. Tharaux, G. Mosser, P.-F. Brevet, and M.-C. Schanne-Klein "Measurement of the quadratic hyperpolarizability of the collagen triple helix and application to second harmonic imaging of natural and biomimetic collagenous tissues", Proc. SPIE 7487, Optical Materials in Defence Systems Technology VI, 74870E (24 September 2009); https://doi.org/10.1117/12.829882

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
6 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

Biomimetics

Microscopy

Data modeling

Nonlinear response

Show All Keywords

Keywords/Phrases

Search In:

Publication Years