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A\u03b2 peptides are amphipathic molecules that can modulate membrane mechanics. Because the mechanosensitive cation channel PIEZO1 is gated by membrane tension and curvature, it prompted us to test the effects of A\u03b2 on PIEZO1. Using precision fluid shear stress as a stimulus, we found that A\u03b2\n                    <jats:italic>monomers<\/jats:italic>\n                    inhibit PIEZO1 at femtomolar to picomolar concentrations. The A\u03b2 oligomers proved much less potent. The effect of A\u03b2s on Piezo gating did not involve peptide-protein interactions since the D and L enantiomers had similar effects. Incubating a fluorescent derivative of A\u03b2 and a fluorescently tagged PIEZO1, we showed that A\u03b2 can colocalize with PIEZO1, suggesting that they both had an affinity for particular regions of the bilayer. To better understand the PIEZO1 inhibitory effects of A\u03b2, we examined their effect on wound healing. We observed that over-expression of PIEZO1 in HEK293 cells\n                    <jats:italic>increased<\/jats:italic>\n                    cell migration velocity ~10-fold, and both enantiomeric A\u03b2 peptides and GsMTx4 independently inhibited migration, demonstrating involvement of PIEZO1 in cell motility. As part of the motility study we examined the correlation of PIEZO1 function with tension in the cytoskeleton using a genetically encoded fluorescent stress probe. A\u03b2 peptides\n                    <jats:italic>increased<\/jats:italic>\n                    resting stress in F-actin, and is correlated with A\u03b2 block of PIEZO1-mediated Ca\n                    <jats:sup>2+<\/jats:sup>\n                    influx. A\u03b2 inhibition of PIEZO1 in the absence of\n                    <jats:italic>stereospecific<\/jats:italic>\n                    peptide-protein interactions shows that A\u03b2 peptides modulate both cell membrane and cytoskeletal mechanics to control PIEZO1-triggered Ca\n                    <jats:sup>2+<\/jats:sup>\n                    influx.\n                  <\/jats:p>","DOI":"10.1038\/s41598-018-32572-2","type":"journal-article","created":{"date-parts":[[2018,9,18]],"date-time":"2018-09-18T07:22:04Z","timestamp":1537255324000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":83,"title":["Enantiomeric A\u03b2 peptides inhibit the fluid shear stress response of PIEZO1"],"prefix":"10.1038","volume":"8","author":[{"given":"Mohammad M.","family":"Maneshi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lynn","family":"Ziegler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4324-2240","authenticated-orcid":false,"given":"Frederick","family":"Sachs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4410-697X","authenticated-orcid":false,"given":"Susan Z.","family":"Hua","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3764-9885","authenticated-orcid":false,"given":"Philip A.","family":"Gottlieb","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2018,9,24]]},"reference":[{"key":"32572_CR1","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1038\/nrn2808","volume":"11","author":"VE Johnson","year":"2010","unstructured":"Johnson, V. 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