Abstract
β-Amino acids are being increasingly used in the design of bioactive ligands and more recently in the generation of novel biomaterials. Peptides containing either individual β-amino acid substitutions or peptides comprised entirely of β-amino acids, display unique properties in terms of their structural and/or chemical characteristics. β-Peptides form well-defined secondary structures that exhibit different geometries compared to the corresponding α-peptides. β-Peptides, including α-peptides containing only one or two β-amino acids, can be easily modified with different functional groups and are metabolically stable and, together with the predictable side chain topography, have led to the design of a growing number of bioactive β-peptides with a range of biological targets and therapeutic applications. More recently, our understanding of the folding and self-assembly of β-peptides has resulted in the generation of novel biomaterials. The focus of this review is to examine how the structural and chemical properties of β-peptides have been exploited in the design of bioactive peptides and selfassembled nanomaterials.
Keywords: β-Peptides, β-amino acids, peptidomimetic, bioactive ligand, proteolytic stability, self-assembly, biomaterials.
Current Pharmaceutical Design
Title:Using β-Amino Acids and β-Peptide Templates to Create Bioactive Ligands and Biomaterials
Volume: 23 Issue: 26
Author(s): Mark P Del Borgo, Ketav Kulkarni and Marie-Isabel Aguilar*
Affiliation:
- Biomedicine Discovery Institute & Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, Vic. 3800,Australia
Keywords: β-Peptides, β-amino acids, peptidomimetic, bioactive ligand, proteolytic stability, self-assembly, biomaterials.
Abstract: β-Amino acids are being increasingly used in the design of bioactive ligands and more recently in the generation of novel biomaterials. Peptides containing either individual β-amino acid substitutions or peptides comprised entirely of β-amino acids, display unique properties in terms of their structural and/or chemical characteristics. β-Peptides form well-defined secondary structures that exhibit different geometries compared to the corresponding α-peptides. β-Peptides, including α-peptides containing only one or two β-amino acids, can be easily modified with different functional groups and are metabolically stable and, together with the predictable side chain topography, have led to the design of a growing number of bioactive β-peptides with a range of biological targets and therapeutic applications. More recently, our understanding of the folding and self-assembly of β-peptides has resulted in the generation of novel biomaterials. The focus of this review is to examine how the structural and chemical properties of β-peptides have been exploited in the design of bioactive peptides and selfassembled nanomaterials.
Export Options
About this article
Cite this article as:
Del Borgo P Mark, Kulkarni Ketav and Aguilar Marie-Isabel *, Using β-Amino Acids and β-Peptide Templates to Create Bioactive Ligands and Biomaterials, Current Pharmaceutical Design 2017; 23 (26) . https://dx.doi.org/10.2174/1381612823666170616083031
DOI https://dx.doi.org/10.2174/1381612823666170616083031 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
- 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
- Announcements
Related Articles
-
Effect of Glycine on Adipocyte Hypertrophy in a Metabolic Syndrome Rat Model
Current Drug Delivery Clinical and Molecular Perspectives of Monogenic Hypertension
Current Hypertension Reviews Food-derived Bioactive Peptides - Opportunities for Designing Future Foods
Current Pharmaceutical Design Angiogenesis-regulating microRNAs and Ischemic Stroke
Current Vascular Pharmacology Evolution of Copper Transporting ATPases in Eukaryotic Organisms
Current Genomics Vanilloid Receptor Antagonists: Emerging Class of Novel Anti-Inflammatory Agents for Pain Management
Current Pharmaceutical Design Vascular and Metabolic Actions of the Green Tea Polyphenol Epigallocatechin Gallate
Current Medicinal Chemistry Editorial (Thematic Issue: The Crosstalk between Non-Pharmaceutical and Pharmaceutical Approaches to Prevention and Treatment of Chronic Diseases: Current Concepts and Perspectives)
Current Pharmaceutical Design Vitamin D and Vitamin D Receptor Activators in Treatment of Hypertension and Cardiovascular Disease
Cardiovascular & Hematological Disorders-Drug Targets Heat Shock Paradox and a New Role of Heat Shock Proteins and their Receptors as Anti-Inflammation Targets
Inflammation & Allergy - Drug Targets (Discontinued) A Brief History of ‘Lone’ Atrial Fibrillation: From ‘A Peculiar Pulse Irregularity’ to a Modern Public Health Concern
Current Pharmaceutical Design The Podocyte: a Potential Therapeutic Target in Diabetic Nephropathy?
Current Pharmaceutical Design Pulmonary Complications After Congenital Heart Surgery
Current Respiratory Medicine Reviews Angiotensin Receptor Blockers in Hypertension and Cardiovascular Diseases
Cardiovascular & Hematological Agents in Medicinal Chemistry Adaptive Filtering of the Arterial Wall: Frequency Response and Dynamical Parameters: Clinical Evaluation
Current Hypertension Reviews Quality Based Design Approach for Improving Oral Bioavailability of Valsartan Loaded Smedds And Study of Impact of Lipolysis on the Drug Diffusion
Drug Delivery Letters T9-T10 Osteomyelitis, Epidural Abscess and Cord Compression Secondary to <i>Mycobacterium abscessus</i>: A Case Report
Infectious Disorders - Drug Targets CYP Epoxygenase Derived EETs: From Cardiovascular Protection to Human Cancer Therapy
Current Topics in Medicinal Chemistry Chickpea (Cicer arietinum L.) Lectin Exhibit Inhibition of ACE-I, α-amylase and α-glucosidase Activity
Protein & Peptide Letters Endothelin-1 and Human Platelets
Current Vascular Pharmacology