Intramolecularly stapled amphipathic peptides<i>via</i>a boron–sugar interaction

Kijewska, Monika; Czerwińska, A; Al-Harthi, Samah; Wołczański, Grzegorz; Waliczek, Mateusz; Emwas, Abdul‐Hamid; Jaremko, Mariusz; Jaremko, Łukasz; Stefanowicz, Piotr; Szewczuk, Zbigniew

doi:10.1039/d0cc02603d

Cited by 6 publications

(8 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Szewczuk and co-workers reported the intramolecular interaction between the fructosyl moiety and phenylboronic acid (PhB) and its application in peptide stapling. 120 Specifically, the linear resin-bound peptides bearing deoxyfructosylated Lys moiety (Fmoc-Lys(i,i-Fru,Boc)−OH) and Fmoc-Lys(Mtt)−OH at i, i+4 or i, i+7 or i, i+11 or i, i+15 position were smoothly obtained by SPPS. The latter Lys residue was selectively deprotected and then the PhB was incorporated.…”

Section: I I+3mentioning

confidence: 99%

“…In this case, helical amphipathic penetrating peptide and C-terminus peptide of RNaseA were used as the models, and the resulting stapled peptides showed higher helical contents than the linear peptides. 120 2.4. Lys-Cys via Thio-Addition or Diels−Alder Reaction 2.4.1.…”

Section: I I+3mentioning

confidence: 99%

“…The final TFA cleavage (in acidic condition) would simultaneously resulted in stable intramolecular interaction between Fru and PhB, thus affording the stapled peptides with different ring sizes in moderate to good yields (Scheme ). In this case, helical amphipathic penetrating peptide and C -terminus peptide of RNaseA were used as the models, and the resulting stapled peptides showed higher helical contents than the linear peptides …”

Section: Stapling Two Natural Amino Acidsmentioning

confidence: 99%

See 2 more Smart Citations

Stapled Helical Peptides Bearing Different Anchoring Residues

et al. 2020

View full text Add to dashboard Cite

A large proportion of protein–protein interactions (PPIs) occur between a short peptide and a globular protein domain; the peptides involved in surface interactions play important roles, and there is great promise for using peptide motifs to interfere with protein interactions. Peptide inhibitors show more promise in blocking large surface protein interactions compared to small molecule inhibitors. However, peptides have drawbacks including poor stability against circulating proteolytic enzymes and an intrinsic inability to penetrate cell membranes. Stapled helical peptides, by adopting a preformed, stable α-helical conformation, exhibit improved proteolytic stability and membrane permeability compared to linear bioactive peptides. In this review, we summarize the broad aspects of peptide stapling for chemistry, biophysics, and biological applications and specifically highlight the methodology by providing an inventory of different anchoring residues categorized into two natural amino acids, two nonnatural amino acids, or a combination of natural and nonnatural amino acids. Additional advantages of specific peptide stapling techniques, including but not limited to reversibility, bio-orthogonal reactivity, and photoisomerization, are also discussed individually. This review is expected to provide a broad reference for the rational design of druggable stapled peptides targeting therapeutic proteins, particularly those involved in PPIs, by considering the impact of anchoring residues, functional cross-linkers, physical staple length, staple components, and the staple motif on the biophysical properties of the peptides.

show abstract

Section: I I+3mentioning

confidence: 99%

Section: I I+3mentioning

confidence: 99%

Section: Stapling Two Natural Amino Acidsmentioning

confidence: 99%

See 1 more Smart Citation

Stapled Helical Peptides Bearing Different Anchoring Residues

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Most boric acid ester chemical processes produce water rather than proton [10] . The one releasing proton is the case of boric acid and polyols under ambient condition, although they are usually used for analytical chemistry [11] . Hence, it can be envisioned that this boric acid ester chemistry is utilized to generate proton gradients as the driving force for bioenergy conversion.…”

Section: Figurementioning

confidence: 99%

Boric Acid‐Fueled ATP Synthesis by F_oF₁ATP Synthase Reconstituted in a Supramolecular Architecture

Fei

et al. 2021

Angewandte Chemie

View full text Add to dashboard Cite

Significant strides toward producing biochemical fuels have been achieved by mimicking natural oxidative and photosynthetic phosphorylation. Here, different from these strategies, we explore boric acid as a fuel for tuneable synthesis of energy-storing molecules in a cell-like supramolecular architecture. Specifically, a proton locked in boric acid is released in a modulated fashion by the choice of polyols. As a consequence, controlled proton gradients across the lipid membrane are established to drive ATP synthase embedded in the biomimetic architecture, which facilitates tuneable ATP production. This strategy paves a unique route to achieve highly efficient bioenergy conversion, holding broad applications in synthesis and devices that require biochemical fuels.

show abstract

“…NMR can be used in reaction kinetic studies while several consecutive measurements are taken, and while spectral changes (function of the reaction time) are analyzed [ 24 , 25 , 26 , 27 , 28 ]. Moreover, molecules are studied at the atomic level [ 29 , 30 , 31 ]. Unlike other analytical tools, NMR provides dynamic information, and NMR experiments can be carried out under physiological conditions (e.g., atmospheric pressure, temperature, and different pH values) [ 32 , 33 ].…”

Section: Introductionmentioning

confidence: 99%

NMR as a “Gold Standard” Method in Drug Design and Discovery

et al. 2020

Self Cite

View full text Add to dashboard Cite

Studying disease models at the molecular level is vital for drug development in order to improve treatment and prevent a wide range of human pathologies. Microbial infections are still a major challenge because pathogens rapidly and continually evolve developing drug resistance. Cancer cells also change genetically, and current therapeutic techniques may be (or may become) ineffective in many cases. The pathology of many neurological diseases remains an enigma, and the exact etiology and underlying mechanisms are still largely unknown. Viral infections spread and develop much more quickly than does the corresponding research needed to prevent and combat these infections; the present and most relevant outbreak of SARS-CoV-2, which originated in Wuhan, China, illustrates the critical and immediate need to improve drug design and development techniques. Modern day drug discovery is a time-consuming, expensive process. Each new drug takes in excess of 10 years to develop and costs on average more than a billion US dollars. This demonstrates the need of a complete redesign or novel strategies. Nuclear Magnetic Resonance (NMR) has played a critical role in drug discovery ever since its introduction several decades ago. In just three decades, NMR has become a “gold standard” platform technology in medical and pharmacology studies. In this review, we present the major applications of NMR spectroscopy in medical drug discovery and development. The basic concepts, theories, and applications of the most commonly used NMR techniques are presented. We also summarize the advantages and limitations of the primary NMR methods in drug development.

show abstract

Intramolecularly stapled amphipathic peptidesviaa boron–sugar interaction

Abstract:
The intramolecular interactions between the fructosyl moiety and phenylboronic acid incorporated into various positions of the peptide chain were investigated using mass spectrometry (MS), circular dichroism (CD), and nuclear magnetic resonance (NMR).

Cited by 6 publications

References 28 publications

Stapled Helical Peptides Bearing Different Anchoring Residues

Stapled Helical Peptides Bearing Different Anchoring Residues

Boric Acid‐Fueled ATP Synthesis by F_oF₁ATP Synthase Reconstituted in a Supramolecular Architecture

NMR as a “Gold Standard” Method in Drug Design and Discovery

Contact Info

Product

Resources

About

Intramolecularly stapled amphipathic peptidesviaa boron–sugar interaction

Abstract: The intramolecular interactions between the fructosyl moiety and phenylboronic acid incorporated into various positions of the peptide chain were investigated using mass spectrometry (MS), circular dichroism (CD), and nuclear magnetic resonance (NMR).

Cited by 6 publications

References 28 publications

Stapled Helical Peptides Bearing Different Anchoring Residues

Stapled Helical Peptides Bearing Different Anchoring Residues

Boric Acid‐Fueled ATP Synthesis by FoF1ATP Synthase Reconstituted in a Supramolecular Architecture

NMR as a “Gold Standard” Method in Drug Design and Discovery

Contact Info

Product

Resources

About

Abstract:
The intramolecular interactions between the fructosyl moiety and phenylboronic acid incorporated into various positions of the peptide chain were investigated using mass spectrometry (MS), circular dichroism (CD), and nuclear magnetic resonance (NMR).

Boric Acid‐Fueled ATP Synthesis by F_oF₁ATP Synthase Reconstituted in a Supramolecular Architecture