Trypsin inhibitors in plants

Chen, Ingrid; Mitchell, H. L.

doi:10.1016/0031-9422(73)80013-5

Cited by 32 publications

(13 citation statements)

References 7 publications

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“…Substances that inhibit proteinase (proteolytic enzymes) are present in most organs, biological fluids, and endogenous secretions of man and animals (71). Potatoes, sweet corn, many fruits and vegetables (72), cereals (73), and peanuts (74) possess very high TI activity.…”

Section: Natural Occurrencementioning

confidence: 99%

Biological and physiological factors in soybeans

Rackis

1974

J Americ Oil Chem Soc

203

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There are limitations to which one is justified in drawing broad generalizations concerning the diverse biological and physiological effects of soy protein products. Nevertheless, there appear to be two distinct situations: (A.) Proper heat treatment exerts TI activity b 66-233 c Hemagglutinating activity 60-426 d Protein efficiency ratio 0.88-1.60 e Protein efficiency ratio 0.74-1.74 f aSee ref. 9. bTI = trypsin inhibitor. CExpressed as trypsin units inhibited/rag protein.162A

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Section: Natural Occurrencementioning

confidence: 99%

Biological and physiological factors in soybeans

Rackis

1974

J Americ Oil Chem Soc

203

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“…Corn trypsin inhibitor (CTI) or corn Hageman factor inhibitor is a bifunctional serine protease and a-amylase inhibitor [9][10][11][12][13][14]. It was first isolated from corn in the 1970s, and shown to have inhibitory activity against trypsin [12,[15][16][17][18][19]. Subsequently, CTI was shown to potently inhibit FXIIa and moderately inhibit FXIa with selectivity over activated FX (FXa), thrombin, and kallikrein [10,11,14,16,17,20].…”

Section: Introductionmentioning

confidence: 99%

Assessment of the protein interaction between coagulation factor XII and corn trypsin inhibitor by molecular docking and biochemical validation

Hamad

Pathak

Manna

et al. 2017

Journal of Thrombosis and Haemostasis

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Essentials Corn Trypsin Inhibitor (CTI) is a selective inhibitor of coagulation Factor XII (FXII).Molecular modelling of the CTI‐FXIIa complex suggested a canonical inhibitor binding mode.Mutagenesis revealed the CTI inhibitory loop and helices α1 and α2 mediate the interaction.This confirms that CTI inhibits FXII in canonical fashion and validates the molecular model. SummaryBackgroundCorn trypsin inhibitor (CTI) has selectivity for the serine proteases coagulation factor XII and trypsin. CTI is in widespread use as a reagent that specifically inhibits the intrinsic pathway of blood coagulation but not the extrinsic pathway.ObjectivesTo investigate the molecular basis of FXII inhibition by CTI.MethodsWe performed molecular docking of CTI, using its known crystal structure, with a model of the activated FXII (FXIIa) protease domain. The interaction model was verified by use of a panel of recombinant CTI variants tested for their ability to inhibit FXIIa enzymatic activity in a substrate cleavage assay.ResultsThe docking predicted that: (i) the CTI central inhibitory loop P1 Arg34 side chain forms a salt bridge with the FXIIa S1 pocket Asp189 side chain; (ii) Trp22 from CTI helix α1 interacts with the FXIIa S3 pocket; and (iii) Arg43 from CTI helix α2 forms a salt bridge with FXIIa H1 pocket Asp60A. CTI amino acid substitution R34A negated all inhibitory activity, whereas the G32W, L35A, W22A and R42A/R43A substitutions reduced activity by large degrees of 108‐fold, 41‐fold, 158‐fold, and 100‐fold, respectively; the R27A, W37A, W39A and R42A substitutions had no effect. Synthetic peptides spanning CTI residues 20–44 had inhibitory activity that was three‐fold to 4000‐fold less than that of full‐length CTI.ConclusionsThe data confirm the validity of a canonical model of the FXIIa–CTI interaction, with helix α1 (Trp22), central inhibitory loop (Arg34) and helix α2 (Arg43) of CTI being required for effective binding by contacting the S1, S3 and H1 pockets of FXIIa, respectively.

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“…Amide nitrogen content of the meals was determined as described by Bhatty et al (1973) (Pritchard et al 1973 Merr.) (Wolf 1970), kidney beans (Phaseolus vulgaris) (Pusztai 1965) and mung beans (P. aureus) (Hang et al 1970 (Wolf 1970 Pusztai (1965), and in Aqueous extraction of TI was similar to the method used by Chen and Mitchell (1973). Wilson et al (1972) (Nitsan 1971;Wilson et al 1972) Nitsan (1971) and of Wilson et al (1972) …”

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confidence: 99%

Chemical Composition of Some Faba Bean Cultivars

Bhatty¹

1974

Can. J. Plant Sci.

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Trypsin inhibitors in plants

Cited by 32 publications

References 7 publications

Biological and physiological factors in soybeans

Biological and physiological factors in soybeans

Assessment of the protein interaction between coagulation factor XII and corn trypsin inhibitor by molecular docking and biochemical validation

Chemical Composition of Some Faba Bean Cultivars

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