Dear researchers
I can not find the papers that clarify the role of hydrophobic residues including Ala, Leu, Ile, Val, Trp, and Phe in the anticancer peptides( ACPs) activity and in the peptides interaction with the cell membrane . are any references that discuss these subjects ? can I use your guides?
so Thanks
Farid
Dear Farid Nasiri ,
I think a very good starting point might be an excellent paper describing features of ACPs:
Tyagi, A., Kapoor, P., Kumar, R., Chaudhary, K., Gautam, A., & Raghava, G. P. S. (2013). In silico models for designing and discovering novel anticancer peptides. Scientific reports, 3, 2984.
It describes the webserver antiCP:
https://webs.iiitd.edu.in/raghava/anticp/index.html
with on its home page a schematic representation of the different models by which these types of peptides might work. Recently the researchers behind this server launched a new version:
https://webs.iiitd.edu.in/raghava/anticp2/
In the corresponding paper:
https://www.biorxiv.org/content/10.1101/2020.03.23.003780v1.abstract
they give an excellent overview of what is known so far:
“Anticancer peptides (ACPs) are part of the antimicrobial peptide group which exhibits anticancer activity. These are small peptides [5-50 amino acids] and cationic in nature. Mostly they possess α-helix as the secondary structure (e.g. LL-37, BMAP-27, BMAP-28, Cercopin A, etc.) or folds into β-sheet (e.g. Defensins, Lactoferrin, etc.). Some peptides have shown extended linear structure such as Tritrpticin and Indolicidin”.
In:
Dobrzyńska, B. Szachowicz-Petelska, S. Sulkowski, Z. Figaszewski, Changes in electric charge and phospholipids composition in human colorectal cancer cells, Mol. Cell. Biochem. 276 (2005) 113–9. https://doi.org/10.1007/s11010-005-3557-3.
It has been argued that cationic anticancer peptides interact with the negatively charged membrane via electrostatic interactions ultimately leading to selective killing of cancer cells.
In one of the best and most comprehensive review:
Hoskin, D. W., & Ramamoorthy, A. (2008). Studies on anticancer activities of antimicrobial peptides. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1778(2), 357-375.
It looks like that a subset of ACPs are amphipathic helices. This means they have a hydrophilic (positive in this case) and a hydrophobic side. Here you might find what you are looking for. Papers (and references in it) that comes close to what you are looking for might be:
Dennison, S. R., Harris, F., Bhatt, T., Singh, J., & Phoenix, D. A. (2010). A theoretical analysis of secondary structural characteristics of anticancer peptides. Molecular and cellular biochemistry, 333(1-2), 129.
Riedl, S., Zweytick, D., & Lohner, K. (2011). Membrane-active host defense peptides–challenges and perspectives for the development of novel anticancer drugs. Chemistry and physics of lipids, 164(8), 766-781.
Hope this helps you a bit further.
Best regards.
Dear Keller,
I appreciate you because of your comprehensive answer and precious recommended papers. But These papers only describe anticancer peptides and their functions. At the same time, they did not discuss the importance or role of hydrophobic residues in ACPs activity . they could also not propose any molecular mechanism for hydrophobic residues function in ACPs.
Best regards.
I do not fully agree with you. The amphipathic helix has two sides and one is hydrophobic, the extent to which the peptide can insert for example might very well be correlated to the extent of hydrophobicity. There is a wealth of literature available on this fascinating type of helix.
But I agree concrete studies regarding ACPs are hard to find. In the meantime, I did find some. Because of the resemblance between ACPS and antimicrobial peptides the following paper might be of interest:
Role of Peptide Hydrophobicity in the Mechanism of Action of α-Helical Antimicrobial Peptides Yuxin Chen, Michael T. Guarnieri, Adriana I. Vasil, Michael L. Vasil, Colin T. Mant, Robert S. Hodges. Antimicrobial Agents and Chemotherapy Mar 2007, 51 (4) 1398-1406; DOI: 10.1128/AAC.00925-06
https://aac.asm.org/content/51/4/1398
References 106-109 in the following paper deal with hydrophobicity and ACPs are I think exactly what you are looking for:
https://www.mdpi.com/1420-3049/24/10/1973
Good luck!
Reference 107, Surface Physical Activity and Hydrophobicity of Designed Helical Peptide Amphiphiles Control Their Bioactivity and Cell Selectivity, is a useful paper. So so thanks for your notable suggestions.
Best respects
increased hydrophobicity triggers the self-association of peptides that cause two different consequences based on the cell type. Peptides self-association reduces the antimicrobial potential of peptides, while it is able to enhance the anticancer activity of sequences.
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