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1.
Sci Rep ; 8(1): 12002, 2018 08 07.
Article in English | MEDLINE | ID: mdl-30087381

ABSTRACT

A correction to this article has been published and is linked from the HTML and PDF versions of this paper. The error has been fixed in the paper.

2.
Sci Rep ; 7(1): 15150, 2017 11 09.
Article in English | MEDLINE | ID: mdl-29123121

ABSTRACT

The photoelastic phenomenon has been widely investigated as a fundamental elastooptical property of solids. This effect has been applied extensively to study stress distribution in lattice-mismatched semiconductor heterostructures. GaAs based optoelectronic devices (e.g. solar cells, modulators, detectors, and diodes) used in space probes are subject to damage arising from energetic proton (H+) irradiation. For that reason, the effect of proton irradiation on photoelastic coefficients of GaAs is of primary importance to space applied optoelectronics. However, there yet remains a lack of systematic studies of energetic proton induced changes in the photoelastic properties of bulk GaAs. In this work, the H+ energy and fluence chosen for GaAs implantation are similar to that of protons originating from the radiation belts and solar flares. We present the depth-dependent photoelastic coefficient P 12 profile in non-annealed H+ implanted GaAs obtained from the analysis of the time-domain Brillouin scattering spectra. The depth-dependent profiles are found to be broader than the defect distribution profiles predicted by Monte Carlo simulations. This fact indicates that the changes in photoelastic coefficient P 12 depend nonlinearly on the defect concentrations created by the hydrogen implantation. These studies provide insight into the spatial extent to which defects influence photoelastic properties of GaAs.

3.
Biophys J ; 95(3): 1371-81, 2008 Aug.
Article in English | MEDLINE | ID: mdl-18441025

ABSTRACT

Tissue ablation with mid-infrared irradiation tuned to collagen vibrational modes results in minimal collateral damage. The hypothesis for this effect includes selective scission of protein molecules and excitation of surrounding water molecules, with the scission process currently favored. In this article, we describe the postablation infrared spectral decay kinetics in a model collagen-like peptide (Pro-Pro-Gly)(10). We find that the decay is exponential with different decay times for other, simpler dipeptides. Furthermore, we find that collagen-like polypeptides, such as (Pro-Pro-Gly)(10), show multiple decay times, indicating multiple scission locations and cross-linking to form longer chain molecules. In combination with data from high-resolution mass spectrometry, we interpret these products to result from the generation of reactive intermediates, such as free radicals, cyanate ions, and isocyanic acid, which can form cross-links and protein adducts. Our results lead to a more complete explanation of the reduced collateral damage resulting from infrared laser irradiation through a mechanism involving cross-linking in which collagen-like molecules form a network of cross-linked fibers.


Subject(s)
Collagen/chemistry , Collagen/radiation effects , Models, Chemical , Models, Molecular , Peptides/chemistry , Peptides/radiation effects , Collagen/ultrastructure , Computer Simulation , Electrons , Infrared Rays , Lasers , Radiation Dosage
4.
Bosn J Basic Med Sci ; 4(2): 17-21, 2004 May.
Article in English | MEDLINE | ID: mdl-15629018

ABSTRACT

In this paper we present chemically highly resolved images obtained with Scanning Near-field Optical Microscopy (SNOM) coupled with an Infrared (IR) Free Electron Laser (FEL) at Vanderbilt University, Nashville, USA. Main principles governing SNOM imaging as well as essential components of the experimental setup are described. Chemically resolved images showing the distribution of different phases within the boron-nitride films are presented. Universal character of the experiment and its huge potential applications in biophysics and medical sciences domain are illustrated with highly resolved SNOM images of pancreatic cells.


Subject(s)
Microscopy, Atomic Force/methods , Spectrophotometry, Infrared/methods , Animals , Cell Line , Nanotechnology , Pancreas/ultrastructure , Rats
5.
Biophys J ; 85(4): 2705-10, 2003 10.
Article in English | MEDLINE | ID: mdl-14507733

ABSTRACT

The infrared (IR) absorption of a biological system can potentially report on fundamentally important microchemical properties. For example, molecular IR profiles are known to change during increases in metabolic flux, protein phosphorylation, or proteolytic cleavage. However, practical implementation of intracellular IR imaging has been problematic because the diffraction limit of conventional infrared microscopy results in low spatial resolution. We have overcome this limitation by using an IR spectroscopic version of scanning near-field optical microscopy (SNOM), in conjunction with a tunable free-electron laser source. The results presented here clearly reveal different chemical constituents in thin films and biological cells. The space distribution of specific chemical species was obtained by taking SNOM images at IR wavelengths (lambda) corresponding to stretch absorption bands of common biochemical bonds, such as the amide bond. In our SNOM implementation, this chemical sensitivity is combined with a lateral resolution of 0.1 micro m ( approximately lambda/70), well below the diffraction limit of standard infrared microscopy. The potential applications of this approach touch virtually every aspect of the life sciences and medical research, as well as problems in materials science, chemistry, physics, and environmental research.


Subject(s)
Bacteria/cytology , Bacteria/metabolism , Islets of Langerhans/cytology , Islets of Langerhans/metabolism , Microscopy, Confocal/instrumentation , Microscopy, Confocal/methods , Spectrophotometry, Infrared/instrumentation , Spectrophotometry, Infrared/methods , Animals , Biofilms/growth & development , Cell Line , Equipment Failure Analysis , Rats
6.
J Biomed Opt ; 8(2): 216-22, 2003 Apr.
Article in English | MEDLINE | ID: mdl-12683847

ABSTRACT

Light scattering is used to monitor the dynamics and energy thresholds of laser-induced structural alterations in biopolymers due to irradiation by a free electron laser (FEL) in the infrared (IR) wavelength range 2.2 to 8.5 microm. Attenuated total reflectance (ATR) Fourier-transform IR (FTIR) spectroscopy is used to examine infrared tissue absorption spectra before and after irradiation. Light scattering by bovine and porcine cartilage and cornea samples is measured in real time during FEL irradiation using a 650-nm diode laser and a diode photoarray with time resolution of 10 ms. The data on the time dependence of light scattering in the tissue are modeled to estimate the approximate values of kinetic parameters for denaturation as functions of laser wavelength and radiant exposure. We found that the denaturation threshold is slightly lower for cornea than for cartilage, and both depend on laser wavelength. An inverse correlation between denaturation thresholds and the absorption spectrum of the tissue is observed for many wavelengths; however, for wavelengths near 3 and 6 microm, the denaturation threshold does not exhibit the inverse correlation, instead being governed by heating kinetics of tissue. It is shown that light scattering is useful for measuring the denaturation thresholds and dynamics for different biotissues, except where the initial absorptivity is very high.


Subject(s)
Cornea/chemistry , Cornea/radiation effects , Lasers , Nasal Septum/chemistry , Nasal Septum/radiation effects , Proteins/chemistry , Spectroscopy, Fourier Transform Infrared/methods , Absorption , Cartilage/chemistry , Cartilage/physiology , Cartilage/radiation effects , Cornea/physiology , Dose-Response Relationship, Radiation , Electrons , Light , Models, Biological , Nasal Septum/physiology , Protein Denaturation/radiation effects , Proteins/metabolism , Tomography, Optical/methods
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