Role of Short Peptides as an Important Nutritional Element in Maintenance of Body Homeostasis

Peptides are fragments of proteins that carry out biological functions. They act as signaling entities via all domains of life and interfere with protein-protein interactions, which are indispensable in bio-processes. Short peptides include fundamental molecular information for a prelude to the symphony of life. They have aroused considerable interest due to their unique features and great promise in innovative bio-therapies. This work focusing on the current state-of-the-art short peptide-based therapeutical developments is the first global review written by researchers from all continents, as a celebration of 100 years of peptide therapeutics since the commencement of insulin therapy in the 1920s. Peptide “drugs” initially played only the role of hormone analogs to balance disorders. Nowadays, they achieve numerous biomedical tasks, can cross membranes, or reach intracellular targets. The role of peptides in bio-processes can hardly be mimicked by other chemical substances. The article is divided into independent sections, which are related to either the progress in short peptide-based theranostics or the problems posing challenge to bio-medicine. In particular, the SWOT analysis of short peptides, their relevance in therapies of diverse diseases, improvements in (bio)synthesis platforms, advanced nano-supramolecular technologies, aptamers, altered peptide ligands and in silico methodologies to overcome peptide limitations, modern smart bio-functional materials, vaccines, and drug/gene-targeted delivery systems are discussed.

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The Glycine- and Proline-Rich Protein AtGPRP3 Negatively Regulates Plant Growth in Arabidopsis

International Journal of Molecular Sciences ◽

10.3390/ijms21176168 ◽

2020 ◽

Vol 21 (17) ◽

pp. 6168

Author(s):

Xiaojing Liu ◽

Xin Wang ◽

Xin Yan ◽

Shaobo Li ◽

Hui Peng

Keyword(s):

Amino Acids ◽

Plant Growth ◽

Physiological Role ◽

Short Peptides ◽

Hydrophobic Domain ◽

Gfp Fusion Protein ◽

Repeat Domain ◽

Arabidopsis Plant ◽

Proline Rich Protein

Glycine- and proline-rich proteins (GPRPs) comprise a small conserved family that is widely distributed in the plant kingdom. GPRPs are relatively short peptides (<200 amino acids) that contain three typical domains, including an N-terminal XYPP-repeat domain, a middle hydrophobic domain rich in alanine, and a C-terminal HGK-repeat domain. These proteins have been proposed to play fundamental roles in plant growth and environmental adaptation, but their functions remain unknown. In this study, we selected an Arabidopsis GPRP (AtGPRP3) to profile the physiological role of GPRPs. Transcripts of AtGPRP3 could be detected in the whole Arabidopsis plant, but greater amounts were found in the rosette, followed by the cauline. The AtGPRP3::GFP fusion protein was mainly localized in the nucleus. The overexpression and knockout of AtGPRP3, respectively, retarded and accelerated the growth of Arabidopsis seedlings, while the increase in the growth rate of atgprp3 plants was offset by the complementary expression of AtGPRP3. CAT2 and CAT3, but not CAT1, interacted with AtGPRP3 in the nuclei of Arabidopsis protoplasts. The knockout of CAT2 by CRISPR-Cas9 retarded the growth of the Arabidopsis seedlings. Together, our data suggest that AtGPRP3 negatively regulates plant growth, potentially through CAT2 and CAT3.

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Two plant signalling peptides: systemin and ENOD 40.

Acta Biochimica Polonica ◽

10.18388/abp.1997_4384 ◽

1997 ◽

Vol 44 (4) ◽

pp. 795-802 ◽

Cited By ~ 3

Author(s):

J Barciszewski ◽

A B Legocki

Keyword(s):

Biological Role ◽

Short Peptides

Recently several new evidences have appeared on biological role of native short peptides. This is an overview on two of them occurring in plants: systemin and ENOD 40.

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Identification of peptides interfering the lrrk2/pp1 interaction

10.1101/807487 ◽

2019 ◽

Author(s):

Chang Zhi Dong ◽

Heriberto Bruzzoni-Giovanell ◽

Yanhua Yu ◽

Karim Dorgham ◽

Christophe Parizot ◽

...

Keyword(s):

Biological Activity ◽

Elisa Test ◽

Short Peptides ◽

Cell Penetrating Peptide ◽

Original Sequence ◽

Pathological Conditions ◽

Cell Penetrating

ABSTRACTSerine/threonine phosphatases are responsible for counteracting the effect of the protein kinases implicated in the development of several pathologies. Here we identified by PEP-scan approach the sequence of a fragment of LRRK2, a Parkinson’s disease associated protein, interacting with the phosphatase PP1. The fragment, that is located in a LRRK2 domain of undefined function, was associated in N-terminal to an optimized cell penetrating peptide in order to study their in vitro and in vivo biological activity. From this original sequence, we developed and studied five interfering peptides (IPs) and identified two peptides able to disrupt the LRRK2/PP1 interaction by in vitro competition in anti-LRRK2 immunoprecipitates. Using FITC-labelled peptides, we confirmed the internalization of the peptides in cell lines as well as in and primary human normal and pathological cells. Finally, we have confirmed by ELISA test the association of Mut3DPT-LRRK2-Long and Mut3DPT-LRRK2-Short peptides to purified PP1 protein in a selective manner. The shortest peptides, MuteDPT-LRRK2-5 to 8 with either N or C-terminal deletions are not able neither disrupt the association LRRK2/PP1 nor to associate to purified PP1 protein. The peptides Mut3DPT-LRRK2-Long and Mut3DPT-LRRK2-Short may be new tools to study the role of LRRK2/PP1 interaction in normal and pathological conditions.

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Steps Towards the Formation of A Protocell: The Possible Role of Short Peptides

Origins of Life and Evolution of Biospheres ◽

10.1007/s11084-007-9111-4 ◽

2007 ◽

Vol 37 (6) ◽

pp. 537-553 ◽

Cited By ~ 23

Author(s):

Maya Fishkis

Keyword(s):

Short Peptides

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Role of Peptide Bond in the Realization of Biological Activity of Short Peptides

Bulletin of Experimental Biology and Medicine ◽

10.1007/s10517-015-2805-0 ◽

2015 ◽

Vol 158 (4) ◽

pp. 551-554

Author(s):

V. Kh. Khavinson ◽

S. I. Tarnovskaya ◽

N. S. Lin’kova ◽

N. A. Chervyakova ◽

T. E. Nichik ◽

...

Keyword(s):

Biological Activity ◽

Peptide Bond ◽

Short Peptides

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Affinity interactions of human immunoglobulin G with short peptides: role of ligand spacer on binding, kinetics, and mass transfer

Analytical and Bioanalytical Chemistry ◽

10.1007/s00216-015-9135-y ◽

2015 ◽

Vol 408 (7) ◽

pp. 1829-1841 ◽

Cited By ~ 10

Author(s):

Fei Shen ◽

Orlando J. Rojas ◽

Jan Genzer ◽

Patrick V. Gurgel ◽

Ruben G. Carbonell

Keyword(s):

Mass Transfer ◽

Immunoglobulin G ◽

Binding Kinetics ◽

Human Immunoglobulin ◽

Short Peptides ◽

Human Immunoglobulin G

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Synthetic peptides mimicking antigenic epitope of Helicobacter pylori urease.

Acta Biochimica Polonica ◽

10.18388/abp.2006_3365 ◽

2006 ◽

Vol 53 (1) ◽

pp. 83-86 ◽

Cited By ~ 4

Author(s):

Magdalena Białek ◽

Sebastian Grabowski ◽

Zbigniew Kamiński ◽

Wiesław Kaca

Keyword(s):

Helicobacter Pylori ◽

Glutamic Acid ◽

Aspartic Acid ◽

Synthetic Peptides ◽

Short Peptides ◽

Antigenic Epitope ◽

Jack Bean Urease ◽

Jack Bean ◽

H Pylori

Short peptides resembling the Helicobacter pylori urease antigen (UreB F8 Ser-Ile-Lys-Glu-Asp-Val-Gln-Phe) with deleted aspartic acid and glutamic acid residues, anchored through a triazine linker via the N-terminal moiety to cellulose plate were prepared. The peptides were used for binding of antibodies from sera of patients with medically confirmed atherosclerosis. Recognition of the peptides was also tested with anti-Jack beans urease antibodies. The important role of a Gly-Gly spacer separating the peptides from the cellulose support was shown. Different patterns of binding of antibodies from H. pylori infected patients and anti-Jack bean urease antibodies were observed only in the case of pentapeptides. The peptide Gly-Gly-Leu-Val-Phe-Lys-Thr was recognized by most of the tested sera.

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Functional Analysis of Adipokinetic Hormone Signaling in Bombyx mori

Cells ◽

10.3390/cells9122667 ◽

2020 ◽

Vol 9 (12) ◽

pp. 2667

Author(s):

Hana Sehadova ◽

Yoko Takasu ◽

Anna Zaloudikova ◽

Yu-Hsien Lin ◽

Ivo Sauman ◽

...

Keyword(s):

Bombyx Mori ◽

Energy Homeostasis ◽

Fat Body ◽

The Other ◽

Short Peptides ◽

Hormone Signaling ◽

Lipid Levels ◽

Adipokinetic Hormone ◽

Energy Stores

Insect adipokinetic hormones (AKHs) are short peptides produced in the corpora cardiaca and are responsible for mobilizing energy stores from the fat body to the hemolymph. Three related peptides, AKH1, AKH2, and AKH/corazonin-related peptide (ACP) as well as three AKH receptors have been reported in Bombyx mori. AKH1 and AKH2 are specific for the AKHR1 receptor, whereas ACP interacts with the other two AKHRs. To assess the effect of the two silkworm AKHs and ACP in the regulation of energy homeostasis we examined the expression pattern of the three peptides and their receptors as well as their effect on the level of carbohydrates and lipids in the hemolymph. Our results support the hypothesis that only AKH1 and AKH2 peptides together with the AKHR1 receptor are involved in the maintenance of energy homeostasis. Because Bombyx AKHR1 (BmAKHR1) seems to be a true AKHR we generated its mutation. The BmAKHR1 mutant larvae display significantly lower carbohydrate and lipid levels in the hemolymph and reduced sensitivity to starvation. Our study clarifies the role of BmAKHR1 in energy homeostasis.

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