Interaction between wheat alpha-amylase/trypsin bi-functional inhibitor and mammalian digestive enzymes: Kinetic, equilibrium and structural characterization of binding.

Abstract:

:Alpha-amylase/trypsin bi-functional inhibitors (ATIs) are non-gluten protein components of wheat and other cereals that can hypersensitise the human gastrointestinal tract, eventually causing enteropathies in predisposed individuals. These inhibitory proteins can act both directly by targeting specific pro-inflammatory receptors, and indirectly by impairing the activity of digestive enzymes, the latter event causing the accumulation of undigested peptides with potential immunogenic properties. Herein, according to a concerted approach based on in vitro and in silico methods we characterized kinetics, equilibrium parameters and modes of binding of the complexes formed between wheat ATI and two representative mammalian digestive enzymes, namely trypsin and alpha-amylase. Interestingly, we demonstrated ATI to target both enzymes with independent binding sites and with moderately high affinity.

journal_name

Food Chem

journal_title

Food chemistry

authors

Cuccioloni M,Mozzicafreddo M,Ali I,Bonfili L,Cecarini V,Eleuteri AM,Angeletti M

doi

10.1016/j.foodchem.2016.07.020

subject

Has Abstract

pub_date

2016-12-15 00:00:00

pages

571-578

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(16)31044-5

journal_volume

213

pub_type

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