depsipeptide

A depsipeptide is a peptide in which one or more of its amide, -C(O)NHR-, groups are replaced by the corresponding ester, -C(O)OR-.{{GoldBookRef|title=depsipeptides|file=D01604}} Many depsipeptides have both peptide and ester linkages.{{cite journal |last1=Avan |first1=Ilker |last2=Tala |first2=Srinivasa R. |last3=Steel |first3=Peter J. |last4=Katritzky |first4=Alan R. |title=Benzotriazole-Mediated Syntheses of Depsipeptides and Oligoesters |journal=The Journal of Organic Chemistry |date=17 June 2011 |volume=76 |issue=12 |pages=4884–4893 |doi=10.1021/jo200174j |pmid=21452874 |url=https://pubs.acs.org/doi/10.1021/jo200174j|url-access=subscription }} Elimination of the N–H group in a peptide structure results in a decrease of H-bonding capability, which is responsible for secondary structure and folding patterns of peptides, thus inducing structural deformation of the helix and β-sheet structures.{{cite journal |last1=Avan |first1=Ilker |last2=Hall |first2=C. Dennis |last3=Katritzky |first3=Alan R. |title=Peptidomimetics via modifications of amino acids and peptide bonds |journal=Chemical Society Reviews |date=2014 |volume=43 |issue=10 |pages=3575–3594 |doi=10.1039/C3CS60384A |pmid=24626261 |url=https://pubs.rsc.org/en/content/articlelanding/2014/cs/c3cs60384a|url-access=subscription }} Because of decreased resonance delocalization in esters relative to amides, depsipeptides have lower rotational barriers for cis-trans isomerization and therefore they have more flexible structures than their native analogs. They are mainly found in marine and microbial natural products.{{cite journal|title=Recent Progress of the Synthetic Studies of Biologically Active Marine Cyclic Peptides and Depsipeptides|author=Yasumasa Hamada |author2=Takayuki Shioiri |journal=Chem. Rev.|year=2005|volume=105|issue=12|pages=4441–4482|doi=10.1021/cr0406312|pmid=16351050}}

File:Depsipeptide Principle V.1.png

Depsipeptide natural products

file:Enterobactin.svg is a depsipeptide that is an iron-transporter.{{cite journal |author=Walsh |author2=Christopher T. |author3=Jun Liu |author4=Frank Rusnak |author5=Masahiro Sakaitani | title = Molecular Studies on Enzymes in Chorismate Metabolism and the Enterobactin Biosynthetic Pathway | journal = Chemical Reviews | volume = 90 | year = 1990 | pages = 1105–1129 | doi = 10.1021/cr00105a003 | issue = 7}}]]

Several depsipeptides have been found to exhibit anti-cancer properties.{{cite journal|journal=Anticancer Drugs|year=2015|volume=26|pages=259–71| doi=10.1097/CAD.0000000000000183|title=Cyclic depsipeptides as potential cancer therapeutics|author1=Kitagaki, J. |author2=Shi, G. |author3=Miyauchi, S. |author4=Murakami, S. |author5=Yang, Y. |issue=3|pmid=25419631 |s2cid=22071968 }}

A depsipeptide enzyme inhibitor includes romidepsin, a member of the bicyclic peptide class, a known histone deacetylase inhibitors (HDACi). It was first isolated as a fermentation product from Chromobacterium violaceum by the Fujisawa Pharmaceutical Company.{{cite journal | doi = 10.1021/jm0703800 | title = The First Biologically Active Synthetic Analogues of FK228, the Depsipeptide Histone Deacetylase Inhibitor | year = 2007 | last1 = Yurek-George | first1 = Alexander | last2 = Cecil | first2 = Alexander Richard Liam | last3 = Mo | first3 = Alex Hon Kit | last4 = Wen | first4 = Shijun | last5 = Rogers | first5 = Helen | last6 = Habens | first6 = Fay | last7 = Maeda | first7 = Satoko | last8 = Yoshida | first8 = Minoru | last9 = Packham | first9 = Graham | last10 = Ganesan | first10 = A. | journal = Journal of Medicinal Chemistry | volume = 50 | issue = 23 | pages = 5720–5726 | pmid = 17958342| display-authors = 8 }}

Streptogramins, specifically streptogramin B antibiotics, are depsipeptides that bind to the 50S subunit of bacterial ribosomes.{{cite book |doi=10.1016/B978-0-444-53717-1.01472-4 |quote=Streptogramins [1] are a class of antibiotics of two types, streptogramin A and streptogramin B. Separately, group A and group B streptogramins are bacteriostatic, by reversible binding to the 50S subunit of 70S bacterial ribosomes. Together, however, streptogramins from each group are synergic and bactericidal. |chapter=Streptogramins |title=Meyler's Side Effects of Drugs |date=2016 |page=499 |isbn=978-0-444-53716-4 |editor1-first=J.K. |editor1-last=Aronson }}

Etamycin was shown in preliminary data in 2010 to have potent activity against MRSA in a mouse model.{{cite journal | journal = Journal of Antibiotics | volume = 63 | year = 2010 | pages = 219–24 | doi = 10.1038/ja.2010.22 | title = Activity of the streptogramin antibiotic etamycin against methicillin-resistant Staphylococcus aureus | last1 = Haste | first1 = Nina M | last2 = Perera | first2 = Varahenage R | last3 = Maloney | first3 = Katherine N | last4 = Tran | first4 = Dan N | last5 = Jensen | first5 = Paul | last6 = Fenical | first6 = William | last7 = Nizet | first7 = Victor | last8 = Hensler | first8 = Mary E | issue = 5| pmc = 2889693 | pmid=20339399}}

Several depsipeptides from Streptomyces exhibit antimicrobial activity.K. H. Michel, R. E. Kastner (Eli Lilly and Company), US 4492650, 1985 [Chem. Abstr. 1985, 102, 130459]{{cite journal | last1 = Osada | first1 = Hiroyuki | last2 = Yano | first2 = Tatsuya | last3 = Koshino | first3 = Hiroyuki | last4 = Isono | first4 = Kiyoshi | year = 1991 | title = Enopeptin A, a novel depsipeptide antibiotic with anti-bacteriophage activity | journal = The Journal of Antibiotics | volume = 44 | issue = 12| pages = 1463–1466 | doi=10.7164/antibiotics.44.1463| pmid = 1778798 | doi-access = free }} These form a new, potential class of antibiotics known as acyldepsipeptides (ADEPs). ADEPs target and activate the casein lytic protease (ClpP) to initiate uncontrolled peptide and unfolded protein degradation, killing many Gram-positive bacteria.{{cite journal | last1 = Li | last2 = Him Shun | first2 = Dominic | last3 = Guarné | first3 = Alba | last4 = Maurizi | first4 = Michael R. | last5 = Cheng | first5 = Yi-Qiang | last6 = Wright | first6 = Gerard D. | last7 = Ghirlando | first7 = Rodolfo | last8 = Joseph | first8 = Ebenezer | last9 = Gloyd | first9 = Melanie | last10 = Seon Chung | first10 = Yu | last11 = Ortega | first11 = Joaquin | year = 2010 | title = Acyldepsipeptide Antibiotics Induce The Formation Of A Structured Axial Channel In ClpP: A Model For The ClpX/ClpA-Bound State Of ClpP | journal = Chemistry & Biology | volume = 17 | issue = 9| pages = 959–969 | doi=10.1016/j.chembiol.2010.07.008 | pmid = 20851345 | pmc = 2955292}}{{cite journal | last1 = Hinzen | first1 = Berthold | author-link3 = Heike Brötz-Oesterhelt | last2 = Labischinski | first2 = Harald | last3 = Brötz-Oesterhelt | first3 = Heike | last4 = Endermann | first4 = Rainer | last5 = Benet-Buchholz | first5 = Jordi | last6 = Hellwig | first6 = Veronica | last7 = Häbich | first7 = Dieter | last8 = Schumacher | first8 = Andreas | last9 = Lampe | first9 = Thomas | last10 = Paulsen | first10 = Holger | last11 = Raddatz | first11 = Siegfried | year = 2006 | title = Medicinal Chemistry Optimization of Acyldepsipeptides of the Enopeptin Class Antibiotics | journal = ChemMedChem | volume = 1 | issue = 7| pages = 689–693 | doi=10.1002/cmdc.200600055 | pmid = 16902918| s2cid = 36525372 }}{{cite journal | last1 = Carney | first1 = Daniel W. | last2 = Schmitz | first2 = Karl R. | last3 = Truong | first3 = Jonathan V. | last4 = Sauer | first4 = Robert T. | last5 = Sello | first5 = Jason K. | year = 2014 | title = Restriction of the Conformational Dynamics of the Cyclic Acyldepsipeptide Antibiotics Improves Their Antibacterial Activity | journal = Journal of the American Chemical Society | volume = 136 | issue = 5 | pages = 1922–1929 | doi=10.1021/ja410385c| pmid = 24422534 | pmc = 4004210 | doi-access = free }}

Depsipeptides can be formed through a Passerini reaction.{{Citation |last=Li |first=Jie Jack |title=Passerini Reaction |date=2021 |url=http://link.springer.com/10.1007/978-3-030-50865-4_115 |work=Name Reactions |pages=424–426 |place=Cham |publisher=Springer International Publishing |language=en |doi=10.1007/978-3-030-50865-4_115 |isbn=978-3-030-50864-7 |access-date=2022-10-26|url-access=subscription }}

depsipeptide

Depsipeptide natural products

References

Further reading