Cell-Penetrating Helical Peptides Having l-Arginines and Five-Membered Ring α,α-Disubstituted α-Amino Acids

2014 ◽  
Vol 25 (10) ◽  
pp. 1761-1768 ◽  
Author(s):  
Takuma Kato ◽  
Makoto Oba ◽  
Koyo Nishida ◽  
Masakazu Tanaka
Keyword(s):  
Amino Acids ◽  
Membered Ring ◽  
Helical Peptides ◽  
Cell Penetrating

Tropolone-Based Treatments for Visualising Latent Fingermarks on Porous Surfaces

2019 ◽  
Author(s):  
Clara M. Agapie ◽  
Melissa Sampson ◽  
William Gee
Keyword(s):  
Amino Acids ◽  
Uv Radiation ◽  
Membered Ring ◽  
Diazonium Salts ◽  
Chemical Detection ◽  
Latent Fingerprints ◽  
Porous Surfaces

The work describes a new chemical means of visualising latent fingerprints (fingermarks) using tropolone. Tropolone reacts with amino acids within the fingermark residue to form adducts that absorb UV radiation. These adducts provide useful contrast on highly-fluorescent prous surfaces will illuminated with UV radiation. The conjugated seven-membered ring of the tropolone adduct can be reacted further diazonium salts, which is demonstrated here with formation of two dyes. The methodology is extremely rapid, occurring in minutes with mild heating, and can be applied before ninhydrin in a chemical detection sequence. <br>

scholarly journals Helical structures of l-Leu-based peptides having chiral six-membered ring amino acids

Tetrahedron ◽  
2016 ◽  
Vol 72 (22) ◽  
pp. 3124-3131 ◽  
Author(s):  
Tomohiro Umeno ◽  
Atsushi Ueda ◽  
Makoto Oba ◽  
Mitsunobu Doi ◽  
Takayuki Hirata ◽  
...  
Keyword(s):  
Amino Acids ◽  
Membered Ring ◽  
Helical Structures

Cell-Penetrating, Dimeric α-Helical Peptides: Nanomolar Inhibitors of HIV-1 Transcription

2014 ◽  
Vol 53 (38) ◽  
pp. 10086-10089 ◽  
Author(s):  
Sangmok Jang ◽  
Soonsil Hyun ◽  
Seoyeon Kim ◽  
Seonju Lee ◽  
Im-Soon Lee ◽  
...  
Keyword(s):  
Helical Peptides ◽  
Cell Penetrating ◽  
Hiv 1

Development of helix-stabilized cell-penetrating peptides containing cationic α,α-disubstituted amino acids as helical promoters

2017 ◽  
Vol 25 (6) ◽  
pp. 1846-1851 ◽  
Author(s):  
Hiroko Yamashita ◽  
Takashi Misawa ◽  
Makoto Oba ◽  
Masakazu Tanaka ◽  
Mikihiko Naito ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating ◽  
Disubstituted Amino Acids

Stereochemistry as a determining factor for the effect of a cell-penetrating peptide on cellular viability and epithelial integrity

2018 ◽  
Vol 475 (10) ◽  
pp. 1773-1788 ◽  
Author(s):  
Ditlev Birch ◽  
Malene V. Christensen ◽  
Dan Staerk ◽  
Henrik Franzyk ◽  
Hanne Mørck Nielsen
Keyword(s):  
Amino Acids ◽  
Cell Viability ◽  
Mammalian Cells ◽  
Membrane Integrity ◽  
Cell Penetrating Peptides ◽  
Proliferating Cells ◽  
Epithelial Integrity ◽  
Cell Penetrating ◽  
Culture Models ◽  
Well Differentiated

Cell-penetrating peptides (CPPs) comprise efficient peptide-based delivery vectors. Owing to the inherent poor enzymatic stability of peptides, CPPs displaying partial or full replacement of l-amino acids with the corresponding d-amino acids might possess advantages as delivery vectors. Thus, the present study aims to elucidate the membrane- and metabolism-associated effects of l-Penetratin (l-PEN) and its corresponding all-d analog (d-PEN). These effects were investigated when exerted on hepatocellular (HepG2) or intestinal (Caco-2 and IEC-6) cell culture models. The head-to-head comparison of these enantiomeric CPPs included evaluation of their effects on cell viability and morphology, epithelial membrane integrity, and cellular ultrastructure. In all investigated cell models, a rapid decrease in cell viability, pronounced membrane perturbation and an altered ultrastructure were detected upon exposure to d-PEN. At equimolar concentrations, these observations were less pronounced or even absent for cells exposed to l-PEN. Both CPPs remained stable for at least 2 h during exposure to proliferating cells (cultured for 24 h), although d-PEN exhibited a longer half-life when compared with that of l-PEN when exposed to well-differentiated cell monolayers (cultured for 18–20 days). Thus, the stereochemistry of the CPP penetratin significantly influences its effects on cell viability and epithelial integrity when profiled against a panel of mammalian cells.

Enhanced and Prolonged Cell-Penetrating Abilities of Arginine-Rich Peptides by Introducing Cyclic α,α-Disubstituted α-Amino Acids with Stapling

2017 ◽  
Vol 28 (7) ◽  
pp. 1801-1806 ◽  
Author(s):  
Makoto Oba ◽  
Masayuki Kunitake ◽  
Takuma Kato ◽  
Atsushi Ueda ◽  
Masakazu Tanaka
Keyword(s):  
Amino Acids ◽  
Cell Penetrating

ChemInform Abstract: Synthesis of New Seven-Membered Ring Cyclic Dipeptides from Functionalized β-Amino Acids.

ChemInform ◽  
2010 ◽  
Vol 31 (14) ◽  
pp. no-no
Author(s):  
Ouafaa El Mahdi ◽  
Jean-Pierre Lavergne ◽  
Jean Martinez ◽  
Philippe Viallefont ◽  
E. M. Essassi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Membered Ring ◽  
Cyclic Dipeptides

Plasmid DNA delivery by arginine-rich cell-penetrating peptides containing unnatural amino acids

2016 ◽  
Vol 24 (12) ◽  
pp. 2681-2687 ◽  
Author(s):  
Takuma Kato ◽  
Hiroko Yamashita ◽  
Takashi Misawa ◽  
Koyo Nishida ◽  
Masaaki Kurihara ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasmid Dna ◽  
Unnatural Amino Acids ◽  
Dna Delivery ◽  
Cell Penetrating Peptides ◽  
Cell Penetrating

scholarly journals Method to generate highly stable D-amino acid analogs of bioactive helical peptides using a mirror image of the entire PDB

2018 ◽  
Vol 115 (7) ◽  
pp. 1505-1510 ◽  
Author(s):  
Michael Garton ◽  
Satra Nim ◽  
Tracy A. Stone ◽  
Kyle Ethan Wang ◽  
Charles M. Deber ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Data Bank ◽  
Mirror Image ◽  
Proof Of Concept ◽  
Human Gut ◽  
Helical Peptides ◽  
Peptide Engineering ◽  
Small Molecule Drugs ◽  
Proteins And Peptides

Biologics are a rapidly growing class of therapeutics with many advantages over traditional small molecule drugs. A major obstacle to their development is that proteins and peptides are easily destroyed by proteases and, thus, typically have prohibitively short half-lives in human gut, plasma, and cells. One of the most effective ways to prevent degradation is to engineer analogs from dextrorotary (D)-amino acids, with up to 105-fold improvements in potency reported. We here propose a general peptide-engineering platform that overcomes limitations of previous methods. By creating a mirror image of every structure in the Protein Data Bank (PDB), we generate a database of ∼2.8 million D-peptides. To obtain a D-analog of a given peptide, we search the (D)-PDB for similar configurations of its critical—“hotspot”—residues. As a proof of concept, we apply our method to two peptides that are Food and Drug Administration approved as therapeutics for diabetes and osteoporosis, respectively. We obtain D-analogs that activate the GLP1 and PTH1 receptors with the same efficacy as their natural counterparts and show greatly increased half-life.

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