title: ÐÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ðµ ÑÑÑÑÐºÑÑÑÐ½ÑÑ Ð¾ÑÐ¾Ð±ÐµÐ½Ð½Ð¾ÑÑÐµÐ¹ Ð±Ð¸Ð¾ÐºÐ¾Ð¼Ð¿Ð¾Ð·Ð¸ÑÐ¾Ð² Ð½Ð° Ð¾ÑÐ½Ð¾Ð²Ðµ ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð¾Ð² I, IV Ð¸ V ÑÐ¸Ð¿Ð¾Ð² Ð¼ÐµÑÐ¾Ð´Ð¾Ð¼ ÐÐ-Ð¤ÑÑÑÐµ ÑÐ¿ÐµÐºÑÑÐ¾ÑÐºÐ¾Ð¿Ð¸Ð¸
title: Ð²ÑÐ¿ÑÑÐºÐ½Ð°Ñ ÐºÐ²Ð°Ð»Ð¸ÑÐ¸ÐºÐ°ÑÐ¸Ð¾Ð½Ð½Ð°Ñ ÑÐ°Ð±Ð¾ÑÐ° Ð±Ð°ÐºÐ°Ð»Ð°Ð²ÑÐ°
titleType: Subtitle
title: Study of structural features biocomposites based on collagens of types I, IV and V by FTIR spectroscopy
Creators: name: ÐÐ¾Ð»Ð¾ÑÐ¾Ð²Ð°, ÐÐ»ÐµÑÑ
Publisher: name: Ð¡Ð°Ð½ÐºÑ-ÐÐµÑÐµÑÐ±ÑÑÐ³ÑÐºÐ¸Ð¹ Ð¿Ð¾Ð»Ð¸ÑÐµÑÐ½Ð¸ÑÐµÑÐºÐ¸Ð¹ ÑÐ½Ð¸Ð²ÐµÑÑÐ¸ÑÐµÑ ÐÐµÑÑÐ° ÐÐµÐ»Ð¸ÐºÐ¾Ð³Ð¾
Year: 2023
Subjects: ÑÐ¸Ð¿Ñ ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð°
Ð±Ð¸Ð¾ÐºÐ¾Ð¼Ð¿Ð¾Ð·Ð¸ÑÑ
ÐÐ-Ð¤ÑÑÑÐµ ÑÐ¿ÐµÐºÑÑÐ¾ÑÐºÐ¾Ð¿Ð¸Ñ
ÑÐ¸Ð±ÑÐ¸Ð»Ð¾Ð¾Ð±ÑÐ°Ð·Ð¾Ð²Ð°Ð½Ð¸Ðµ
ÐºÐ¾Ð»ÐµÐ±Ð°Ð½Ð¸Ñ
ÑÐµÐ»Ð¾Ð¿ÐµÐ¿ÑÐ¸Ð´Ñ
Ð²Ð¸Ð´Ð¾Ð²Ð¾Ðµ Ð¿ÑÐ¾Ð¸ÑÑ Ð¾Ð¶Ð´ÐµÐ½Ð¸Ðµ
Ð²ÑÐ¾ÑÐ¸ÑÐ½Ð°Ñ ÑÑÑÑÐºÑÑÑÐ° Ð±ÐµÐ»ÐºÐ°
types of collagen
biocomposites
FTIR
fibril formation
oscillations
telopeptides
species origin
secondary protein structure

description: ÐÑÐ¿ÑÑÐºÐ½Ð°Ñ ÐºÐ²Ð°Ð»Ð¸ÑÐ¸ÐºÐ°ÑÐ¸Ð¾Ð½Ð½Ð°Ñ ÑÐ°Ð±Ð¾ÑÐ° Ð¿Ð¾ÑÐ²ÑÑÐµÐ½Ð° Ð°Ð½Ð°Ð»Ð¸Ð·Ñ ÑÑÑÑÐºÑÑÑÐ½ÑÑ Ð¾ÑÐ¾Ð±ÐµÐ½Ð½Ð¾ÑÑÐµÐ¹ Ð±Ð¸Ð¾ÐºÐ¾Ð¼Ð¿Ð¾Ð·Ð¸ÑÐ¾Ð² Ð½Ð° Ð¾ÑÐ½Ð¾Ð²Ðµ I, IV Ð¸ V ÑÐ¸Ð¿Ð¾Ð² ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð° Ñ Ð¿Ð¾Ð¼Ð¾ÑÑÑ Ð¼ÐµÑÐ¾Ð´Ð° ÐÐ-Ð¤ÑÑÑÐµ ÑÐ¿ÐµÐºÑÑÐ¾ÑÐºÐ¾Ð¿Ð¸Ð¸. Ð ÐºÐ°ÑÐµÑÑÐ²Ðµ Ð¾Ð±ÑÐµÐºÑÐ° Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ñ Ð±ÑÐ»Ð¸ Ð²ÑÐ±ÑÐ°Ð½Ñ Ð¿Ð»ÐµÐ½ÐºÐ¸ Ð²ÑÑÑÑÐµÐ½Ð½ÑÑ ÑÐ°ÑÑÐ²Ð¾ÑÐ¾Ð² ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð°, Ð½Ð°Ð½ÐµÑÐµÐ½Ð½ÑÐµ Ð½Ð° Ð¼ÐµÑÐ°Ð»Ð»Ð¸ÑÐµÑÐºÐ¸Ðµ Ð¿Ð¾Ð´Ð»Ð¾Ð¶ÐºÐ¸. ÐÐ±ÑÐ°Ð·ÑÑ Ð±ÑÐ»Ð¸ Ð¿ÑÐ¸Ð³Ð¾ÑÐ¾Ð²Ð»ÐµÐ½Ñ ÑÐ°Ð·Ð½ÑÐ¼Ð¸ ÑÐ¿Ð¾ÑÐ¾Ð±Ð°Ð¼Ð¸ Ð´Ð»Ñ Ð²Ð¾Ð·Ð¼Ð¾Ð¶Ð½Ð¾ÑÑÐ¸ Ð¸Ð·ÑÑÐµÐ½Ð¸Ñ Ð·Ð°Ð²Ð¸ÑÐ¸Ð¼Ð¾ÑÑÐ¸ ÑÑÑÑÐºÑÑÑÑ ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð° Ð¾Ñ ÐµÐ³Ð¾ ÑÐ¸Ð¿Ð°, pH ÑÐ°ÑÑÐ²Ð¾ÑÐ°, Ð²Ð¸Ð´Ð¾Ð²Ð¾Ð³Ð¾ Ð¿ÑÐ¾Ð¸ÑÑÐ¾Ð¶Ð´ÐµÐ½Ð¸Ñ Ð¸ Ð½Ð°Ð»Ð¸ÑÐ¸Ñ ÑÐµÐ»Ð¾Ð¿ÐµÐ¿ÑÐ¸Ð´Ð¾Ð². ÐÐ»Ñ Ð¿Ð¾ÑÑÑÐ¾ÐµÐ½Ð¸Ñ ÑÐ¿ÐµÐºÑÑÐ¾Ð² Ð¸ÑÐ¿Ð¾Ð»ÑÐ·Ð¾Ð²Ð°Ð½Ð° Ð¿ÑÐ¸ÐºÐ»Ð°Ð´Ð½Ð°Ñ Ð¿ÑÐ¾Ð³ÑÐ°Ð¼Ð¼Ð° Origin. Ð Ð½Ð°ÑÐ°Ð»Ðµ ÑÐ°Ð±Ð¾ÑÑ Ð±ÑÐ»Ð¾ Ð¿ÑÐ¾Ð²ÐµÐ´ÐµÐ½Ð¾ Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ðµ ÑÐ¿ÐµÐºÑÑÐ¾Ð² ÑÐ¸Ð±ÑÐ¸Ð»Ð»ÑÑÐ½Ð¾Ð¹ Ð¸ Ð¼Ð¾Ð»ÐµÐºÑÐ»ÑÑÐ½Ð¾Ð¹ ÑÑÑÑÐºÑÑÑÐ½ÑÑ ÑÐ¾ÑÐ¼ ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð° I ÑÐ¸Ð¿Ð°. ÐÑÑÐ²Ð»ÐµÐ½Ð½ÑÐµ Ð¾ÑÐ»Ð¸ÑÐ¸Ñ Ð² ÑÐ¿ÐµÐºÑÑÐ°Ñ Ð¿Ð¾Ð·Ð²Ð¾Ð»ÑÑÑ ÑÑÐ´Ð¸ÑÑ Ð¾ ÑÑÑÑÐºÑÑÑÐ½ÑÑ Ð¾ÑÐ¾Ð±ÐµÐ½Ð½Ð¾ÑÑÑÑ â Ð¿Ð¾ÑÐ²Ð»ÐµÐ½Ð¸Ð¸ Ð½Ð¾Ð²ÑÑ ÑÐ²ÑÐ·ÐµÐ¹ Ð¿ÑÐ¸ Ð²Ð·Ð°Ð¸Ð¼Ð¾Ð´ÐµÐ¹ÑÑÐ²Ð¸Ð¸. ÐÑÐ¿Ð¾Ð»ÑÐ·ÑÑ Ð¿Ð¾Ð»ÑÑÐµÐ½Ð½ÑÐµ ÑÐµÐ·ÑÐ»ÑÑÐ°ÑÑ, ÑÐ´Ð°Ð»Ð¾ÑÑ Ð¿ÑÐ¾Ð°Ð½Ð°Ð»Ð¸Ð·Ð¸ÑÐ¾Ð²Ð°ÑÑ, Ð¿ÑÐ¸ ÐºÐ°ÐºÐ¸Ñ Ð·Ð½Ð°ÑÐµÐ½Ð¸ÑÑ pH ÑÐ°ÑÑÐ²Ð¾ÑÐ° Ð¿ÑÐ¾Ð¸ÑÑÐ¾Ð´Ð¸Ñ Ð¾Ð±ÑÐ°Ð·Ð¾Ð²Ð°Ð½Ð¸Ðµ ÑÐ¸Ð±ÑÐ¸Ð»Ð». ÐÐ°Ð½Ð½ÑÐ¹ ÑÐµÐ·ÑÐ»ÑÑÐ°Ñ Ð±ÑÐ» Ð¿Ð¾Ð´ÑÐ²ÐµÑÐ¶Ð´ÐµÐ½ Ð Ð­Ð. ÐÐ°Ð»ÐµÐµ Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ðµ Ð±ÑÐ»Ð¾ Ð½Ð°Ð¿ÑÐ°Ð²Ð»ÐµÐ½Ð¾ Ð² ÑÑÐ¾ÑÐ¾Ð½Ñ Ð²ÑÑÐ²Ð»ÐµÐ½Ð¸Ñ Ð¾ÑÐ»Ð¸ÑÐ¸Ð¹ Ð² ÑÑÑÑÐºÑÑÑÐµ ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð° Ð² Ð·Ð°Ð²Ð¸ÑÐ¸Ð¼Ð¾ÑÑÐ¸ Ð¾Ñ ÑÐºÐ°Ð½Ð¸, Ð¸Ð· ÐºÐ¾ÑÐ¾ÑÐ¾Ð¹ Ð¾Ð½ Ð±ÑÐ» Ð¸Ð·Ð²Ð»ÐµÑÐµÐ½. ÐÑÐ¾ÑÐ°Ñ Ð¿Ð¾Ð»Ð¾Ð²Ð¸Ð½Ð° Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ñ ÐºÐ°ÑÐ°ÐµÑÑÑ Ð²ÑÑÐ²Ð»ÐµÐ½Ð¸Ðµ Ð¾ÑÐ»Ð¸ÑÐ¸ÑÐµÐ»ÑÐ½ÑÑ Ð¾ÑÐ¾Ð±ÐµÐ½Ð½Ð¾ÑÑÐµÐ¹ I, IV Ð¸ V ÑÐ¸Ð¿Ð¾Ð² ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð°. ÐÐ¾Ð»ÑÑÐµÐ½Ð½ÑÐµ ÑÐµÐ·ÑÐ»ÑÑÐ°ÑÑ Ð¼Ð¾Ð³ÑÑ Ð±ÑÑÑ Ð¸ÑÐ¿Ð¾Ð»ÑÐ·Ð¾Ð²Ð°Ð½Ñ Ñ ÑÐµÐ»ÑÑ Ð¸Ñ Ð¸Ð´ÐµÐ½ÑÐ¸ÑÐ¸ÐºÐ°ÑÐ¸Ð¸. ÐÐ½Ð°Ð»Ð¸Ð· ÑÐ¼ÐµÑÐ¸ I Ð¸ IV ÑÐ¸Ð¿Ð° Ð±ÑÐ» Ð½ÐµÐ¾Ð±ÑÐ¾Ð´Ð¸Ð¼ Ð´Ð»Ñ Ð¾Ð¿ÑÐµÐ´ÐµÐ»ÐµÐ½Ð¸Ñ ÑÑÑÐµÑÑÐ²Ð¾Ð²Ð°Ð½Ð¸Ñ Ð²Ð·Ð°Ð¸Ð¼Ð¾Ð´ÐµÐ¹ÑÑÐ²Ð¸Ñ Ð¼ÐµÐ¶Ð´Ñ ÑÐ°Ð·Ð½ÑÐ¼Ð¸ ÑÐ°ÑÑÐ²Ð¾ÑÐ°Ð¼Ð¸ ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð°. ÐÐ¾Ð´Ð¾Ð±Ð½ÑÐµ Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ñ Ð´Ð°ÑÑ Ð¿ÐµÑÑÐ¿ÐµÐºÑÐ¸Ð²Ñ Ð² ÑÐ¾Ð·Ð´Ð°Ð½Ð¸Ð¸ in vitro Ð¾ÑÐ³Ð°Ð½Ð¸Ð·Ð¾Ð²Ð°Ð½Ð½ÑÑ ÐºÐ¾Ð»Ð»Ð°Ð³ÐµÐ½Ð¾Ð²ÑÑ ÑÑÑÑÐºÑÑÑ, Ð½Ð°Ð¸Ð±Ð¾Ð»ÐµÐµ Ð¿Ð¾ÑÐ¾Ð¶Ð¸Ñ Ð½Ð° Ð½Ð°ÑÐ¸Ð²Ð½ÑÐµ, ÑÑÐ¾ ÑÐ²Ð»ÑÐµÑÑÑ Ð¾ÑÐ½Ð¾Ð²Ð½Ð¾Ð¹ ÑÐµÐ»ÑÑ ÑÐºÐ°Ð½ÐµÐ²Ð¾Ð¹ Ð¸Ð½Ð¶ÐµÐ½ÐµÑÐ¸Ð¸.
description: The graduation work is dedicated to the analysis of structural features of biocomposites based on collagen type I, IV and V using the method of Fourier transform infrared spectroscopy. Films of dried collagen solutions deposited on metal substrates were selected as the object of the study. The samples were prepared in various ways to study the dependence of the collagen structure on its type, pH of the solution, species origin and the presence of telopeptides. The application program Origin was used to construct the spectra. At the beginning of the work, the spectra of fibrillar and molecular structural forms of type I collagen were studied. The revealed differences in the spectra allow us to judge the structural features â the appearance of new connections during interaction. Using the results obtained, it was possible to analyze at what pH values of the solution the formation of fibrils occurs. This result was confirmed by the SEM. Further, the study was directed towards identifying differences in the structure of collagen depending on the tissue from which it was extracted. The second half of the study concerns finding distinctive features of types I, IV and V of collagen. The obtained results can be used for the purpose of their identification. The analysis of the mixture of type I and IV was necessary to determine the existence of interaction between different collagen solutions. Such studies provide a perspective in the creation in vitro of organized collagen structures that are most similar to native ones, that is the main goal of tissue engineering.