Show simple item record

dc.rights.licenseACS AuthorsChoice License
dc.rights.licenseOpen Access
dc.contributor.authorWang, Feng
dc.contributor.authorLi, Youhua
dc.contributor.authorYu, Lu
dc.contributor.authorZhu, Jinwen
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.date2020
dc.date.accessioned2022-06-23T04:46:03Z
dc.date.available2022-06-23T04:46:03Z
dc.date.issued2020-11-24
dc.identifier.citationAmphiphilic mPEG-modified oligo-phenylalanine nanoparticles chemoenzymatically synthesized via papain, F. Wang, Y. Li, L. Yu, J. Zhu, F. Zhang, R.J. Linhardt, ACS Omega 5, 30336-30347, 2020.
dc.identifier.issn24701343
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5413
dc.identifier.urihttps://doi.org/10.1021/acsomega.0c05076
dc.descriptionACS Omega 5, 30336-30347
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractAmphiphilic mPEG-modified peptide nanoparticles were developed from oligo-phenylalanine (OPhe) nanoparticles (NPs) synthesized via papain. Tyndall effects indicate that OPhe NPs are amphiphobic. Addition of protein perturbants, sodium dodecyl sulfate (SDS), and urea, in the dispersion solution of OPhe NPs can significantly reduce the Rh,m value of NPs, from approximately 749.2 nm to about 200 nm. Therefore, the hydrophobic interaction and hydrogen bonding play major roles in maintaining the aggregation of OPhe NPs. Using the “grafting to” method, the methoxypolyethylene-modified OPhe NPs (mPEG-g-OPhe NPs) were synthesized and characterized by Fourier transform infrared spectroscopy (FTIR), 1H NMR, electrospray ionization mass spectrometry (ESI-MS), and dynamic light scattering (DLS). The attenuated total reflectance (ATR) spectrum of OPhe NPs and mPEG-g-OPhe NPs demonstrate that the secondary structures of these NPs are mainly β-type. mPEG-g-OPhe NPs can self-aggregate into spherical micelles both in water and cyclohexane. Increasing the chain length of the mPEG moiety, the critical micellar concentrations of mPEG-g-OPhe NPs increased in water but decreased in cyclohexane. The light stability, thermal stability, hydrolysis stability, and encapsulation stability of curcumin were significantly promoted by encapsulation in the micelles formed by mPEG-g-OPhe NPs. The protective effects regularly varied with the variations in the mPEG chain length of mPEG-g-OPhe NPs.
dc.languageen_US
dc.language.isoENG
dc.publisherAmerican Chemical Society (ACS)
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofACS Omega
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleAmphiphilic mPEG-modified oligo-phenylalanine nanoparticles chemoenzymatically synthesized via papain
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/acsomega.0c05076
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages30336-30347
rpi.description.volume5


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record