ArticleBiochimica et biophysica acta. Proteins and proteomics2020
The impact of physiological stress conditions on protein structure and trypsin inhibition of serine protease inhibitor Kazal type 1 (SPINK1) and its N34S variant.
Article in Biochimica et biophysica acta. Proteins and proteomics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 17 citations in OpenAlex.
- pH-induced changes in hydrophobicity and key amino acid exposure regulate myoglobin digestibility.Food chemistry: X · 2026Article
- Comprehensive biochemical, molecular and structural characterization of subtilisin with fibrinolytic potential in bioprocessing.Bioresources and bioprocessing · 2025Article
- The application of protease in aquaculture: Prospects for enhancing the aquafeed industry.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2024Review
- Article
- Synergistic inhibition of Pseudomonas fluorescens growth and proteases activities via sodium chlorite-based oxyhalogen.World journal of microbiology & biotechnology · 2022Article
- Structural and Biophysical Insights into SPINK1 Bound to Human Cationic Trypsin.International journal of molecular sciences · 2022Article
- Article
- A Hypothesized Mechanism for Chronic Pancreatitis Caused by the N34S Mutation of Serine Protease Inhibitor Kazal-Type 1 Based on Conformational Studies.Journal of inflammation research · 2021Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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