Hyun, Soonsil Lee, Yuno Jin, Sun Mi Cho, Jane Park, Jeemin Hyeon, Changbong Kim, Key-Sun Lee, Yan Yu, Jaehoon 2024-01-19T22:31:27Z 2024-01-19T22:31:27Z 2021-09-03 2018-07 2374-7943 https://pubs.kist.re.kr/handle/201004/121219 LK-3, an amphipathic dimeric peptide linked by two disulfide bonds, and related isomeric bundles were synthesized, and their cell penetrating abilities were investigated. The measurements using size exclusion chromatography and dynamic light scattering show that LK-3 and its isomers form cell penetrating oligomers. Calculations, performed for various types of peptide isomers, elucidate a strong correlation between the amphipathic character of dimers and cell penetration ability. The results suggest that the amphipathicities of LK-3 and related bundle dimers are responsible for their oligomerization propensities which in turn determine their cell penetrating abilities. The observations made in this study provide detailed information about the mechanism of cell uptake of LK-3 and suggest a plausible insight of the early stage of nanoparticle formation of the cell penetrating amphipathic peptides. English AMER CHEMICAL SOC Oligomer Formation Propensities of Dimeric Bundle Peptides Correlate with Cell Penetration Abilities Article 10.1021/acscentsci.8b00262 1 ACS CENTRAL SCIENCE, v.4, no.7, pp.885 - 893 ACS CENTRAL SCIENCE 4 7 885 893 N scie scopus 000439816200015 2-s2.0-85050512073 Chemistry, Multidisciplinary Chemistry Article HUMAN IMMUNODEFICIENCY VIRUS AMPHIPHILIC PEPTIDES NANOPARTICLE-UPTAKE HYDROPHOBIC MOMENT PROTEIN AGGREGATION INTERNALIZATION CONFORMATION INTERFACE POLARITY cell penetrating peptide oligomer formation propensity amphipathic peptide nanoparticle