NDLI: Calprotectin Pegylation Enhanced Its Physical and Structural Properties

Content Provider	Springer Nature Link
Author	Shahsavari, Abbas Azad, Mehdi Mobarra, Naser Chegini, Koorosh Goodarzvand Gheibi, Nematollah
Copyright Year	2016
Abstract	Calprotectin is member of the S-100 protein family with a wide plethora of intra-and extracellular functions. Anticancer activities, antimicrobial effects and being a qualified disease marker are among the compelling features of this protein to be used as a pharmaceutical agent. However, there are several impediments to applications of protein pharmaceuticals including: proteolytic degradation, short circulating half-life, low solubility and immunogenicity. Pegylation is a common bioconjugation polymer capable of overcoming these drawbacks. Recombinant expression and purification of calprotectin along with its pegylation would result in enhanced pharmaco-dynamic and pharmacokinetic properties. Our florescence spectroscopy and far Ultraviolet-optical density results indicate that pegylation altered the physical and structural properties of the calprotectin to become in a more stable and functionally active state. Due to enhanced pharmacodynamic and pharmacokinetic properties of the calprotectin via pegylation, this study would pave the way for better in vitro and in vivo validations of calprotectin applications in medical practice.
Starting Page	363
Ending Page	370
Page Count	8
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	35
Issue Number	5
e-ISSN	15734943
Language	English
Publisher	Springer US
Publisher Date	2016-10-18
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calprotectin Pegylation UV-CD Fluorescence Bioorganic Chemistry Biochemistry Organic Chemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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