Show simple item record

dc.creatorRaut, Sangram
dc.creatorGarud, Ashwini
dc.creatorNagarajan, Bhavanai
dc.creatorSabnis, Nirupama
dc.creatorRemaley, Alan
dc.creatorFudala, Rafal
dc.creatorGryczynski, Ignacy
dc.creatorGryczynski, Zygmunt
dc.creatorDzyuba, Sergei V.
dc.creatorBorejdo, Julian
dc.creatorLacko, Andras
dc.date.accessioned2021-03-04T19:21:54Z
dc.date.available2021-03-04T19:21:54Z
dc.date.issued2020-03-16
dc.identifier.urihttps://doi.org/10.1124/jpet.119.262899
dc.identifier.urihttps://repository.tcu.edu/handle/116099117/43807
dc.identifier.urihttps://jpet.aspetjournals.org/content/373/1/113
dc.description.abstractReconstituted high-density lipoprotein (HDL) containing apolipoprotein A-I (Apo A-I) mimics the structure and function of endogenous (human plasma) HDL due to its function and potential therapeutic utility in atherosclerosis, cancer, neurodegenerative diseases, and inflammatory diseases. Recently, a new class of HDL mimetics has emerged, involving peptides with amino acid sequences that simulate the the primary structure of the amphipathic alpha helices within the Apo A-I protein. The findings reported in this communication were obtained using a similar amphiphilic peptide (modified via conjugation of a myristic acid residue at the amino terminal aspartic acid) that self-assembles (by itself) into nanoparticles while retaining the key features of endogenous HDL. The studies presented here involve the macromolecular assembly of the myristic acid conjugated peptide (MYR-5A) into nanomicellar structures and its characterization via steady-state and time-resolved fluorescence spectroscopy. The structural differences between the free peptide (5A) and MYR-5A conjugate were also probed, using tryptophan fluorescence, Förster resonance energy transfer (FRET), dynamic light scattering, and gel exclusion chromatography. To our knowledge, this is the first report of a lipoprotein assembly generated from a single ingredient and without a separate lipid component. The therapeutic utility of these nanoparticles (due to their capablity to incorporate a wide range of drugs into their core region for targeted delivery) was also investigated by probing the role of the scavenger receptor type B1 in this process.en_US
dc.language.isoenen_US
dc.publisherASPET
dc.sourceThe Journal of Pharmacology and Experimental Therapeutics
dc.subjectApolipoprotein-A-Ien_US
dc.subjectProtein Secondary Structureen_US
dc.subjectSynthetic Peptide Analogsen_US
dc.subjectHigh-Density-Lipoproteinsen_US
dc.subjectCholesterol Effluxen_US
dc.subjectAntiinflammatory Propertiesen_US
dc.subjectPoor-Prognosisen_US
dc.subjectDeliveryen_US
dc.subjectAtherosclerosisen_US
dc.subjectDoxorubicinen_US
dc.titleProbing the Assembly of HDL Mimetic, Drug Carrying Nanoparticles Using Intrinsic Fluorescenceen_US
dc.typeArticleen_US
dc.rights.holderPublic Domain (US Government Work)
dc.rights.licensePublic Domain
local.collegeCollege of Science and Engineering
local.departmentPhysics & Astronomy
local.departmentChemistry & Biochemistry
local.personsGryczynski, Z. (PHYS); Dzyuba (CHEM)


Files in this item

Thumbnail
Thumbnail
This item appears in the following Collection(s)

Show simple item record