Editing Peptoid (section)

==Applications==
The first demonstration of the use of peptoids was in screening a combinatorial library of diverse peptoids, which yielded novel high-affinity ligands for 7-transmembrane G-protein-couple receptors.<ref name="pmid8064796">{{cite journal | vauthors = Zuckermann RN, Martin EJ, Spellmeyer DC, Stauber GB, Shoemaker KR, Kerr JM, Figliozzi GM, Goff DA, Siani MA, Simon RJ | display-authors = 6 | title = Discovery of nanomolar ligands for 7-transmembrane G-protein-coupled receptors from a diverse N-(substituted)glycine peptoid library | journal = Journal of Medicinal Chemistry | volume = 37 | issue = 17 | pages = 2678–2685 | date = August 1994 | pmid = 8064796 | doi = 10.1021/jm00043a007 }}</ref>

Peptoids have been developed as candidates for a range of different biomedical applications,<ref name="pmid19343235">{{cite journal | vauthors = Fowler SA, Blackwell HE | title = Structure-function relationships in peptoids: recent advances toward deciphering the structural requirements for biological function | journal = Organic & Biomolecular Chemistry | volume = 7 | issue = 8 | pages = 1508–1524 | date = April 2009 | pmid = 19343235 | pmc = 5962266 | doi = 10.1039/b817980h }}</ref><ref name="pmid19479663">{{cite journal | vauthors = Zuckermann RN, Kodadek T | title = Peptoids as potential therapeutics | journal = Current Opinion in Molecular Therapeutics | volume = 11 | issue = 3 | pages = 299–307 | date = June 2009 | pmid = 19479663 | doi =  }}</ref> including antimicrobial agents,<ref name="pmid33807248">{{cite journal | vauthors = Diamond G, Molchanova N, Herlan C, Fortkort JA, Lin JS, Figgins E, Bopp N, Ryan LK, Chung D, Adcock RS, Sherman M, Barron AE | display-authors = 6 | title = Potent Antiviral Activity against HSV-1 and SARS-CoV-2 by Antimicrobial Peptoids | journal = Pharmaceuticals | volume = 14 | issue = 4 | date = March 2021 | page = 304 | pmid = 33807248 | pmc = 8066833 | doi = 10.3390/ph14040304 | doi-access = free }}</ref> synthetic lung surfactants,<ref name="pmid18834153">{{cite journal | vauthors = Brown NJ, Johansson J, Barron AE | title = Biomimicry of surfactant protein C | journal = Accounts of Chemical Research | volume = 41 | issue = 10 | pages = 1409–1417 | date = October 2008 | pmid = 18834153 | pmc = 3270935 | doi = 10.1021/ar800058t }}</ref><ref>{{cite journal | vauthors = Czyzewski AM, McCaig LM, Dohm MT, Broering LA, Yao LJ, Brown NJ, Didwania MK, Lin JS, Lewis JF, Veldhuizen R, Barron AE | display-authors = 6 | title = Effective in vivo treatment of acute lung injury with helical, amphipathic peptoid mimics of pulmonary surfactant proteins | journal = Scientific Reports | volume = 8 | issue = 1 | pages = 6795 | date = May 2018 | pmid = 29717157 | pmc = 5931611 | doi = 10.1038/s41598-018-25009-3 }}</ref> ligands for various proteins including Src Homology 3 ([[SH3 domain]]),<ref name="pmid9851931">{{cite journal | vauthors = Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA | title = Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors | journal = Science | volume = 282 | issue = 5396 | pages = 2088–2092 | date = December 1998 | pmid = 9851931 | doi = 10.1126/science.282.5396.2088 }}</ref> Vascular Endothelial Growth Factor ([[VEGF]]) receptor 2,<ref name="pmid18386897">{{cite journal | vauthors = Udugamasooriya DG, Dineen SP, Brekken RA, Kodadek T | title = A peptoid "antibody surrogate" that antagonizes VEGF receptor 2 activity | journal = Journal of the American Chemical Society | volume = 130 | issue = 17 | pages = 5744–5752 | date = April 2008 | pmid = 18386897 | doi = 10.1021/ja711193x }}</ref> and antibody [[Immunoglobulin G]] biomarkers for the identification of [[Alzheimer's disease]].<ref name="pmid21215375">{{cite journal | vauthors = Reddy MM, Wilson R, Wilson J, Connell S, Gocke A, Hynan L, German D, Kodadek T | display-authors = 6 | title = Identification of candidate IgG biomarkers for Alzheimer's disease via combinatorial library screening | journal = Cell | volume = 144 | issue = 1 | pages = 132–142 | date = January 2011 | pmid = 21215375 | pmc = 3066439 | doi = 10.1016/j.cell.2010.11.054 }}</ref>

Due to their advantageous characteristics as described above, peptoids are also being actively developed for use in nanotechnology,<ref name="pmid20383129">{{cite journal|display-authors=6|vauthors=Nam KT, Shelby SA, Choi PH, Marciel AB, Chen R, Tan L, Chu TK, Mesch RA, Lee BC, Connolly MD, Kisielowski C, Zuckermann RN|date=May 2010|title=Free-floating ultrathin two-dimensional crystals from sequence-specific peptoid polymers|journal=Nature Materials|volume=9|issue=5|pages=454–460|doi=10.1038/nmat2742|pmid=20383129}}</ref> an area in which they may play an important role.<ref name="pmid22180902">{{cite journal|author-link=K. Eric Drexler|vauthors=Drexler KE|date=2011|title=Peptoids at the 7th Summit: toward macromolecular systems engineering|journal=Biopolymers|volume=96|issue=5|pages=537–544|doi=10.1002/bip.21623|pmid=22180902|s2cid=36456597}}</ref>

=== Antimicrobial agents ===
Researchers supported by grants from the [[National Institutes of Health|NIH]] and [[National Institute of Allergy and Infectious Diseases|NIAID]] tested the efficacy of antimicrobial peptoids against antibiotic-resistant strands of ''[[Mycobacterium tuberculosis]]''.<ref name=":0">{{cite journal | vauthors = Kapoor R, Eimerman PR, Hardy JW, Cirillo JD, Contag CH, Barron AE | title = Efficacy of antimicrobial peptoids against Mycobacterium tuberculosis | journal = Antimicrobial Agents and Chemotherapy | volume = 55 | issue = 6 | pages = 3058–3062 | date = June 2011 | pmid = 21464254 | pmc = 3101442 | doi = 10.1128/AAC.01667-10 }}</ref> Antimicrobial peptoids demonstrate a non-specific mechanism of action against the bacterial membrane, one that differs from small-molecule antibiotics that bind to specific receptors (and thus are susceptible to mutations or alterations in bacterial structure). Preliminary results suggested "appreciable activity" against drug-sensitive bacterial strands, leading to a call for more research into the viability of peptoids as a new class of tuberculocidal drugs.<ref name=":0" />

Researchers at the Barron Lab at Stanford University (supported by a [[National Institutes of Health|NIH]] Pioneer Award grant) are currently studying whether upregulation of the human host defense peptide LL-37 or application of antimicrobial treatments based on LL-37 may prevent or treat sporadic Alzheimer’s dementia. Lead researcher Annelise Barron discovered that the innate human defense peptide LL-37 binds to the peptide Ab, which is associated with Alzheimer's disease. Barron's insight is that an imbalance between LL-37 and Ab may be a critical factor affecting AD-associated fibrils and plaques. The project extends focus upon the potential relationship between chronic, oral ''[[P. gingivalis]]'' and herpesvirus (HSV-1) infections to the progression of Alzheimer's dementia.