Abstract
SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar Ki value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors. It has a cyclic backbone that is cross-braced by a single disulfide bridge and a network of hydrogen bonds that result in a well-defined structure. SFTI-1 is amenable to chemical synthesis, allowing for the creation of synthetic variants. Alterations to the structure such as linearising the backbone or removing the disulfide bridge do not reduce the potency of SFTI-1 significantly, and minimising the peptide to as few as nine residues results in only a small decrease in reactivity. The creation of linear variants of SFTI-1 also provides a tool for investigating putative linear precursor peptides. The mechanism of biosynthesis of SFTI-1 is not yet known but it seems likely that it is a gene-coded product that has arisen from a precursor protein that may be evolutionarily related to classic Bowman-Birk inhibitors.
Keywords: bowman-birk inhibitor, circular backbone, cyclic peptide, potent, sfti-1
Current Protein & Peptide Science
Title: Sunflower Trypsin Inhibitor-1
Volume: 5 Issue: 5
Author(s): Michael L.J. Korsinczky, Horst Joachim Schirra and David J. Craik
Affiliation:
Keywords: bowman-birk inhibitor, circular backbone, cyclic peptide, potent, sfti-1
Abstract: SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar Ki value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors. It has a cyclic backbone that is cross-braced by a single disulfide bridge and a network of hydrogen bonds that result in a well-defined structure. SFTI-1 is amenable to chemical synthesis, allowing for the creation of synthetic variants. Alterations to the structure such as linearising the backbone or removing the disulfide bridge do not reduce the potency of SFTI-1 significantly, and minimising the peptide to as few as nine residues results in only a small decrease in reactivity. The creation of linear variants of SFTI-1 also provides a tool for investigating putative linear precursor peptides. The mechanism of biosynthesis of SFTI-1 is not yet known but it seems likely that it is a gene-coded product that has arisen from a precursor protein that may be evolutionarily related to classic Bowman-Birk inhibitors.
Export Options
About this article
Cite this article as:
Korsinczky L.J. Michael, Schirra Joachim Horst and Craik J. David, Sunflower Trypsin Inhibitor-1, Current Protein & Peptide Science 2004; 5 (5) . https://dx.doi.org/10.2174/1389203043379594
DOI https://dx.doi.org/10.2174/1389203043379594 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Editorial (Thematic Issue: The State of Art in the Treatment of Metal Toxicity)
Current Medicinal Chemistry Emerging Use of Nanotechnology in the Treatment of Neurological Disorders
Current Pharmaceutical Design Diabetes Mellitus: Channeling Care through Cellular Discovery
Current Neurovascular Research Alzheimers Disease: From Pathogenesis to Disease-Modifying Approaches
CNS & Neurological Disorders - Drug Targets On the Design of Broad Based Screening Assays to Identify Potential Pharmacological Chaperones of Protein Misfolding Diseases
Current Topics in Medicinal Chemistry Involvement of the Endocannabinoid System in Motor Disorders
Current Medicinal Chemistry - Central Nervous System Agents Biological Predictors of Aging and Potential of FTIR to Study Age-related Diseases and Aging Metabolic Fingerprint
Current Metabolomics Functional Genomics Approach for Identification of Molecular Processes Underlying Neurodegenerative Disorders in Prion Diseases
Current Genomics Blood-Brain Barrier and Breast Cancer Resistance Protein: A Limit to the Therapy of CNS Tumors and Neurodegenerative Diseases
Anti-Cancer Agents in Medicinal Chemistry The Role of Neurogenesis in Neurodegenerative Diseases and its Implications for Therapeutic Development
CNS & Neurological Disorders - Drug Targets MicroRNAs-Based Therapeutic Strategy for Virally Induced Diseases
Current Drug Discovery Technologies Increased Acetylation of Histone H4 at Lysine 12 (H4K12) in Monocytes of Transgenic Alzheimer’s Mice and in Human Patients
Current Alzheimer Research Role of Nitric Oxide Signaling Pathways in Brain Injuries
Current Chemical Biology Receptor for AGEs (RAGE) as Mediator of NF-kB Pathway Activation in Neuroinflammation and Oxidative Stress
CNS & Neurological Disorders - Drug Targets Neuroprotective Effects of Citrus reticulata in Scopolamine-Induced Dementia Oxidative Stress in Rats
CNS & Neurological Disorders - Drug Targets The Role of Extracellular Adenosine in Chemical Neurotransmission in the Hippocampus and Basal Ganglia: Pharmacological and Clinical Aspects
Current Topics in Medicinal Chemistry Editorial (Thematic Issue: Molecular Modeling, Molecular Dynamics and Bioinformatics in Pharmaceutical Design)
Current Pharmaceutical Design Nanotubes at Neural and Immune Synapses
Current Medicinal Chemistry Agonists of the Tissue-Protective Erythropoietin Receptor in the Treatment of Parkinson’s Disease
Current Topics in Medicinal Chemistry Pathological Gambling in Parkinson’s Disease: An Update on Medical Management
Current Psychopharmacology