Transformation of IR spectra of the human lens capsule due to traumatic lens subluxation and correlation with the excised and dried lens capsule under different treatments.

Abstract

Transformation of the secondary conformational structure of the human lens capsule after traumatic lens subluxation in a patient was investigated by Fourier transform infrared (FT-IR) microscopic spectrometry. The result was compared with the IR spectra of type IV collagen in crystalline state, solid film and aqueous solution and those of the excised and dried lens capsule under compression or treated with ethyl alcohol. The results indicate that the IR spectra of the intact human lens capsule after traumatic lens subluxation were the same as those of the rabbit lens capsule, except in the 1,100-1,000 cm-1 proteoglycan region, but were different from those of type IV collagen aqueous solution at the amide I and II bands and the proteoglycan region, although type IV collagen is a predominant component of lens capsule. Two new peaks at 1,054 and 1,023 cm-1 appeared on the IR spectra of the intact human lens capsule and on those of type IV collagen in crystalline state and solid film after compression but not in normal rabbit lens capsule and native type IV collagen. It was also found that all the IR spectra of the excised and dried lens capsule were similar to those of native type IV collagen in crystalline state and solid film.(ABSTRACT TRUNCATED AT 250 WORDS)