dc.creator | Raut, Sangram | |
dc.creator | Garud, Ashwini | |
dc.creator | Nagarajan, Bhavanai | |
dc.creator | Sabnis, Nirupama | |
dc.creator | Remaley, Alan | |
dc.creator | Fudala, Rafal | |
dc.creator | Gryczynski, Ignacy | |
dc.creator | Gryczynski, Zygmunt | |
dc.creator | Dzyuba, Sergei V. | |
dc.creator | Borejdo, Julian | |
dc.creator | Lacko, Andras | |
dc.date.accessioned | 2021-03-04T19:21:54Z | |
dc.date.available | 2021-03-04T19:21:54Z | |
dc.date.issued | 2020-03-16 | |
dc.identifier.uri | https://doi.org/10.1124/jpet.119.262899 | |
dc.identifier.uri | https://repository.tcu.edu/handle/116099117/43807 | |
dc.identifier.uri | https://jpet.aspetjournals.org/content/373/1/113 | |
dc.description.abstract | Reconstituted 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. | |
dc.language.iso | en | en_US |
dc.publisher | ASPET | |
dc.source | The Journal of Pharmacology and Experimental Therapeutics | |
dc.subject | Apolipoprotein-A-I | |
dc.subject | Protein Secondary Structure | |
dc.subject | Synthetic Peptide Analogs | |
dc.subject | High-Density-Lipoproteins | |
dc.subject | Cholesterol Efflux | |
dc.subject | Antiinflammatory Properties | |
dc.subject | Poor-Prognosis | |
dc.subject | Delivery | |
dc.subject | Atherosclerosis | |
dc.subject | Doxorubicin | |
dc.title | Probing the Assembly of HDL Mimetic, Drug Carrying Nanoparticles Using Intrinsic Fluorescence | |
dc.type | Article | |
dc.rights.holder | Public Domain (US Government Work) | |
dc.rights.license | Public Domain | |
local.college | College of Science and Engineering | |
local.department | Physics and Astronomy | |
local.department | Chemistry and Biochemistry | |
local.persons | Gryczynski, Z. (PHYS); Dzyuba (CHEM) | |