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Biomimetic Proteoglycan Interactions with Type I Collagen Investigated via 2D and 3D TEM.

紀錄類型:	書目-語言資料,手稿 : Monograph/item
正題名/作者:	Biomimetic Proteoglycan Interactions with Type I Collagen Investigated via 2D and 3D TEM./
作者:	Moorehead, Carli.
面頁冊數:	1 online resource (98 pages)
附註:	Source: Masters Abstracts International, Volume: 56-05.
Contained By:	Masters Abstracts International56-05(E).
標題:	Materials science. -
電子資源:	click for full text (PQDT)
ISBN:	9780355073874

Biomimetic Proteoglycan Interactions with Type I Collagen Investigated via 2D and 3D TEM.
Moorehead, Carli.

Biomimetic Proteoglycan Interactions with Type I Collagen Investigated via 2D and 3D TEM. - 1 online resource (98 pages)

Source: Masters Abstracts International, Volume: 56-05.

Thesis (M.S.)

Includes bibliographical references

Collagen is one of the leading components in extracellular matrix (ECM), providing durability, structural integrity, and functionality for many tissues. Regulation of collagen fibrillogenesis and degradation is important in the treatment of a number of diseases from orthopedic injuries to genetic deficiencies. Recently, novel, biocompatible, semi-synthetic biomimetic proteoglycans (BPGs) were developed, which consist of an enzymatically resistant synthetic polymer core and natural chondroitin sulfate bristles. It was demonstrated that BPGs affect type I collagen fibrillogenesis in vitro, as reflected by their impact delaying the kinetic formation of gels similar to native PGs. This indicates that the morphology of collagen scaffolds as well as endogenous ECM could also be modulated by these proteoglycan mimics.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2018

Mode of access: World Wide Web

ISBN: 9780355073874Subjects--Topical Terms:

557839
Materials science.
Index Terms--Genre/Form:

554714
Electronic books.

Biomimetic Proteoglycan Interactions with Type I Collagen Investigated via 2D and 3D TEM.
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500 $a Adviser: Michele Marcolongo.
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504 $a Includes bibliographical references
520 $a Collagen is one of the leading components in extracellular matrix (ECM), providing durability, structural integrity, and functionality for many tissues. Regulation of collagen fibrillogenesis and degradation is important in the treatment of a number of diseases from orthopedic injuries to genetic deficiencies. Recently, novel, biocompatible, semi-synthetic biomimetic proteoglycans (BPGs) were developed, which consist of an enzymatically resistant synthetic polymer core and natural chondroitin sulfate bristles. It was demonstrated that BPGs affect type I collagen fibrillogenesis in vitro, as reflected by their impact delaying the kinetic formation of gels similar to native PGs. This indicates that the morphology of collagen scaffolds as well as endogenous ECM could also be modulated by these proteoglycan mimics.
520 $a However, the imaging modality used previously, reflectance confocal microscopy, did not yield the resolution necessary to spatially localize BPGs within the collagen network or investigate the effect of BPGs on the quality of collagen fibrils produced in an in vitro fibrillogenesis model which is important for understanding the method of interaction. Consequently, a histological technique, electron tomography, was adapted and utilized to 3D image the nano-scale structures within this simplified tissue model. BPGs were found to aid in lateral growth and enhance fibril banding periodicity resulting in structures more closely resembling those in tissue, in addition to attaching to the collagen surface despite the lack of a protein core.
533 $a Electronic reproduction. $b Ann Arbor, Mich. : $c ProQuest, $d 2018
538 $a Mode of access: World Wide Web
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