A Global Review on Short Peptides: Frontiers and Perspectives †
Abstract
:1. Introduction
2. Brief History
3. Short Peptides: Definition
4. Frontiers and Prospects of Short Peptides
4.1. Advantages vs. Disadvantages: SWOT Analysis
4.2. To Overcome Shortcomings of Peptides: Mission (Im)possible?
4.2.1. Constrained Amino-Acids as a Molecular “Meccano”
4.2.2. Cyclic Peptides and Mimetics
4.2.3. Ultra-Short Peptides: Less Is More
4.2.4. Nanoengineering and a Supramolecular Approach
5. Synthesis
5.1. Advances in the Synthesis of Short Peptides and Modified Amino Acids
5.2. Short Difficult Peptide Synthesis
6. In Silico Studies
6.1. Geometry Optimization, Conformational Analysis
6.2. Modelling of Short Peptides
6.3. Peptide Interactions with Lipid Bilayers Using Molecular Dynamics Simulations
6.3.1. Peptide Affinity Dependency on Membrane Composition
6.3.2. Free Energy Calculations through a Peptide Reaction Path
6.3.3. Cooperative Effects
7. Peptide-Based Therapies
7.1. Monocyclic, Bicyclic and Tricyclic Cell-Penetrating Peptides as Molecular Transporters
7.2. Short Peptides in Gene Delivery
7.2.1. Targeting Peptides in GDSs
7.2.2. Cell Penetrating Peptides in GDSs
7.2.3. Endosome-Disruptive Peptides in GDSs
7.2.4. Nuclear Localization Peptides in GDSs
7.3. Taking Peptide Aptamers to a New Level
7.4. Peptide-Based Vaccines
7.5. The Role of Short Peptides in Neurodegenerative Therapy
7.6. Immune Modulation Using Altered Peptide Ligands in Autoimmune Diseases
7.7. Relevance of Short Peptides in Stem Cell Research
7.8. Short Peptide-Based Anti-Viral Agents against SARS-CoV-2
7.9. Antimicrobial Lactoferrin-Based Peptides as Anti-COVID-19
7.10. Peptides from Digestion of Proteins
7.11. Nutraceuticals
7.12. Marine Peptides
7.13. Peptide-Based Cosmeceuticals
8. Conclusions and Future Outlook
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
Abbreviations
A | Acidic |
ACE(I) | angiotensin-converting enzyme (inhibitors) |
AchRs | acetylcholine receptors |
AIDS | acquired immune deficiency syndrome |
Alloc | allyloxycarbonyl |
AMPs | antimicrobial peptides |
APCs | antigen presenting cells |
APL | altered peptide ligands |
ARB | angiotensin receptor blockers |
B | basic |
BAP | bioactive peptides |
BOC | butoxycarbonyl |
Bzl | benzyl |
CG | coarse grain |
COVID-19 | coronavirus disease 2019 |
CPPs | cell penetrating peptides |
CSD | Cambridge Structure Database |
CTL | cytotoxic T lymphocyte |
2D | two-dimensional |
3D | three-dimensional |
DH | degree of hydrolysis |
DKP | diketopiperazines |
DNA | deoxyribonucleic acid |
EDTA | ethylenediaminetetraacetic acid |
FAS | fatty acid synthase |
FDA | Food and Drug Administration |
FMOC | fluorenylmethoxycarbonyl |
GALA | glutamic acid–alanine–leucine–alanine |
GAS | group A streptococcus |
GDS | gene delivery system |
GFR | growth factor receptors |
HeLa | human cervical cancer cell line |
HIV | human immunodeficiency virus |
HMG | high motility group |
HMGR | 3-hydroxy-3-methylglutaryl CoA reductase |
HOAt | 1-hydroxy-7-aza-benzotriazole |
HOBt | 1-hydroxy-benzotriazole |
HPLC | high performance liquid chromatography |
IFN | interferon |
IUPAC | International Union of Pure and Applied Chemistry |
LDL | low-density lipoprotein |
LDLR | LDL receptor |
LF | lactoferrin |
LPS | lipopolysaccharide |
LRPs | low density lipoprotein receptors |
LRs | leptin receptors |
MBP | myelin basic protein |
MD | molecular dynamics |
MHC | major histocompatibility complex |
NF | nuclear factor |
NLSs | nuclear localization signals |
NPC | nuclear pore complex |
PDC | pyruvate dehydrogenase complexes |
PEG | polyethylene glycol |
PES | potential energy surface |
PPI | proton-pump inhibitors |
RAS | renin-angiotensin system |
RCSB PDB | Research Collaboratory for Structural Bioinformatics Protein Data Bank |
RGD | arginine–glycine–aspartic acid |
RNA | ribonucleic acid |
SARS-COV-2 | Severe Acute Respiratory Syndrome Coronavirus |
SPPS | solid-phase synthesis |
SREBP2 | sterol regulatory element-binding protein 2 |
SWOT | strengths, weaknesses, opportunities, and threats |
tBu | tert-butyl |
TFA | trifluoroacetic acid |
TFRs | transferrin receptors |
TMC | trimethyl chitosan |
TNF | tumor necrosis factor alpha |
TNFR | tumor necrosis factor receptor 1 |
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Strengths | Weaknesses |
essential bio-molecules with a broad range of activities & functionalities in vivo | instability in vivo (easy degradation in plasma, protease sensitivity) |
bio-chemical diversity, easy availability | short half-life |
structural simplicity | low (oral) bioavailability |
easy design & cost-effective synthesis with high purity | difficult membrane permeability in the case of greater peptides * |
easy modification, scaling up | low binding affinity * |
mechanical stability | high conformational freedom * |
high: modularity, flexibility *, selectivity, target specificity, affinity *, absorbability, potency, tolerability, efficacy, safety, biocompatibility, biodegradibility | |
low toxicity, antigenicity, immunogenicity | |
easy recognition by bio-systems | |
ability to penetrate the cell membranes (but only very short peptides) *, high brain penetration in systematical administration | |
versatility as both targeting moieties and therapeutic agents | |
specific interactions with various bio-systems | |
predictable metabolism: degradation products are amino acids (non-toxic, natural entities used as nutrients or cellular building blocks) | |
lack or fewer secondary off-targets (side) effects (peptides do not accumulate in kidney or liver) | |
low unspecific binding to the structures other than the desired target, minimisation of drug-drug interactions, less accumulation in tissues (low risk of complications due to intermediate metabolites) | |
Opportunities | Threats |
development of peptide-based delivery systems: - cell-penetrating peptides - nano-cyclic peptide-based micceles, vesicles as gene or drug carriers - conjugations with non-peptidic motifs | oncogenicity of endogenous & synthetic peptides |
supramolecular peptide-based biofunctional materials | immunogenicity (related to greater peptides) |
formulations development (e.g., subcutaneous injections)various forms of using (drugs, vaccines, hormones, radioisotopes) | |
development of the peptide-based safe & effective vaccines | |
diveristy of well-ordered, robust, long-lived self-assembled nanostructures | |
vital tool for neurodegenerative diseases studies & various applications in anticancer therapy | |
peptoids or peptidomimetics |
Name of Peptide | No. of Amino Acids |
---|---|
diphenylalanine | 2 |
α,β-dehydrophenylalanine | 2 |
Fmoc-diphenylalanine-konjac glucomannan | 2 |
Ac-EFFAAE-NH2(AIP-1/2) | 6 |
FFKLVFF | 7 |
P11 (QQEFQWQFRQQ) | 11 |
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Apostolopoulos, V.; Bojarska, J.; Chai, T.-T.; Elnagdy, S.; Kaczmarek, K.; Matsoukas, J.; New, R.; Parang, K.; Lopez, O.P.; Parhiz, H.; et al. A Global Review on Short Peptides: Frontiers and Perspectives. Molecules 2021, 26, 430. https://doi.org/10.3390/molecules26020430
Apostolopoulos V, Bojarska J, Chai T-T, Elnagdy S, Kaczmarek K, Matsoukas J, New R, Parang K, Lopez OP, Parhiz H, et al. A Global Review on Short Peptides: Frontiers and Perspectives. Molecules. 2021; 26(2):430. https://doi.org/10.3390/molecules26020430
Chicago/Turabian StyleApostolopoulos, Vasso, Joanna Bojarska, Tsun-Thai Chai, Sherif Elnagdy, Krzysztof Kaczmarek, John Matsoukas, Roger New, Keykavous Parang, Octavio Paredes Lopez, Hamideh Parhiz, and et al. 2021. "A Global Review on Short Peptides: Frontiers and Perspectives" Molecules 26, no. 2: 430. https://doi.org/10.3390/molecules26020430