Chemical modifications of tryptophan residues in peptides and proteins

Hu, Jin-Jian; He, Peng; Li, Yanmei

doi:10.1002/psc.3286

Cited by 46 publications

(14 citation statements)

References 78 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These modifications allow a better understanding of the function post-translational modifications (PTMs) on natural proteins. They also enable the design of improved probes for bioimaging or the optimisation of protein/peptides-based drugs (Hu et al ., 2021).…”

Section: Discussionmentioning

confidence: 99%

Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides

Khemaissa

Walrant

Sagan

2022

Quart. Rev. Biophys.

View full text Add to dashboard Cite

Trp is unique among the amino acids since it is involved in many different types of noncovalent interactions such as electrostatic and hydrophobic ones, but also in π-π, π-cation, π-anion and π-ion pair interactions. In membranotropic peptides and proteins, Trp locates preferentially at the water-membrane interface. In antimicrobial or cell-penetrating peptides (AMPs and CPPs respectively), Trp is well-known for its strong role in the capacity of these peptides to interact and affect the membrane organisation of both bacteria and animal cells at the level of the lipid bilayer. This essential amino acid can however be involved in other types of interactions, not only with lipids, but also with other membrane partners, that are crucial to understand the functional roles of membranotropic peptides. This review is focused on this latter less known role of Trp and describes in details, both in qualitative and quantitative ways: (i) the physico-chemical properties of Trp; (ii) its effect in CPP internalisation; (iii) its importance in AMP activity; (iv) its role in the interaction of AMPs with glycoconjugates or lipids in bacteria membranes and the consequences on the activity of the peptides; (v) its role in the interaction of CPPs with negatively charged polysaccharides or lipids of animal membranes and the consequences on the activity of the peptides. We intend to bring highlights of the physico-chemical properties of Trp and describe its extensive possibilities of interactions, not only at the well-known level of the lipid bilayer, but with other less considered cell membrane components, such as carbohydrates and the extracellular matrix. The focus on these interactions will allow the reader to reevaluate reported studies. Altogether, our review gathers dedicated studies to show how unique are Trp properties, which should be taken into account to design future membranotropic peptides with expected antimicrobial or cell-penetrating activity.

show abstract

Section: Discussionmentioning

confidence: 99%

Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides

Khemaissa

Walrant

Sagan

2022

Quart. Rev. Biophys.

View full text Add to dashboard Cite

show abstract

“…Amino acid or peptide modification has been an important scientific issue and has been applied across many fields, such as organic synthesis, drug delivery, biological probes, and material science . Twenty common α-amino acids have been provided by nature, with aliphatic, aromatic, or polar side chains.…”

mentioning

confidence: 99%

C(sp³)–H/C(sp³)–H Dehydrogenative Radical Coupling of Glycine Derivatives

Wang

Sang

et al. 2022

Org. Lett.

View full text Add to dashboard Cite

show abstract

“…Therefore, modification of other amino acids is also attractive. For example, the functionalization of tryptophan (Trp) [33] and tyrosine (Tyr) [34] can provide site‐specific modifications, as Trp is the rarest amino acid and Tyr is rarely exposed on the surface.…”

Section: Aromatic Amino Acidsmentioning

confidence: 99%

Hypervalent Iodine‐Mediated Late‐Stage Peptide and Protein Functionalization

2021

View full text Add to dashboard Cite

Hypervalent iodine compounds are powerful reagents for the development of novel transformations. As they exhibit low toxicity, high functional group tolerance, and stability in biocompatible media, they have been used for the functionalization of biomolecules. Herein, we report recent advances up to June 2021 in peptide and protein modification using hypervalent iodine reagents. Their use as group transfer or oxidizing reagents is discussed in this Minireview, including methods targeting polar, aromatic, or aliphatic amino acids and peptide termini.

show abstract

Chemical modifications of tryptophan residues in peptides and proteins

Cited by 46 publications

References 78 publications

Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides

Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides

C(sp³)–H/C(sp³)–H Dehydrogenative Radical Coupling of Glycine Derivatives

Hypervalent Iodine‐Mediated Late‐Stage Peptide and Protein Functionalization

Contact Info

Product

Resources

About

Chemical modifications of tryptophan residues in peptides and proteins

Cited by 46 publications

References 78 publications

Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides

Tryptophan, more than just an interfacial amino acid in the membrane activity of cationic cell-penetrating and antimicrobial peptides

C(sp3)–H/C(sp3)–H Dehydrogenative Radical Coupling of Glycine Derivatives

Hypervalent Iodine‐Mediated Late‐Stage Peptide and Protein Functionalization

Contact Info

Product

Resources

About

C(sp³)–H/C(sp³)–H Dehydrogenative Radical Coupling of Glycine Derivatives