The impact of physiological stress conditions on protein structure and trypsin inhibition of serine protease inhibitor Kazal type 1 (SPINK1) and its N34S variant.
Circular dichroism spectroscopy (CD)
Pancreatitis
Serine protease inhibitor Kazal type 1 (SPINK1)
Stress conditions
Surface plasmon resonance (SPR)
Trypsin inhibitor
Journal
Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
22
05
2019
revised:
27
08
2019
accepted:
11
09
2019
pubmed:
17
9
2019
medline:
4
3
2020
entrez:
17
9
2019
Statut:
ppublish
Résumé
One of the most common mutations in the serine protease inhibitor Kazal type 1 (SPINK1) gene is the N34S variant which is strongly associated with chronic pancreatitis. Although it is assumed that N34S mutation constitutes a high-risk factor, the underlying pathologic mechanism is still unknown. In the present study, we investigated the impact of physiological stress factors on SPINK1 protein structure and trypsin inhibitor function using biophysical methods. Our circular dichroism spectroscopy data revealed differences in the secondary structure of SPINK1 and N34S mutant suggesting protein structural changes induced by the mutation as an impairment that could be disease-relevant. We further confirmed that both SPINK1 (K
Identifiants
pubmed: 31525466
pii: S1570-9639(19)30167-0
doi: 10.1016/j.bbapap.2019.140281
pmc: PMC6905150
pii:
doi:
Substances chimiques
SPINK1 protein, human
0
Trypsin Inhibitor, Kazal Pancreatic
50936-63-5
Trypsin
EC 3.4.21.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
140281Informations de copyright
Copyright © 2019 The Author(s). Published by Elsevier B.V. All rights reserved.
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