TY - JOUR
T1 - Branched amphiphilic peptide capsules
T2 - Cellular uptake and retention of encapsulated solutes
AU - Sukthankar, Pinakin
AU - Avila, L. Adriana
AU - Whitaker, Susan K.
AU - Iwamoto, Takeo
AU - Morgenstern, Alfred
AU - Apostolidis, Christos
AU - Liu, Ke
AU - Hanzlik, Robert P.
AU - Dadachova, Ekaterina
AU - Tomich, John M.
N1 - Funding Information:
Partial support for this project was provided by PHS-NIH grants GM 074096 (to J.M.T.) and GM021784 (to R.P.H.) and the Terry Johnson Cancer Center for summer support (to P.S.)
PY - 2014/9
Y1 - 2014/9
N2 - Branched amphiphilic peptide capsules (BAPCs) are peptide nano-spheres comprised of equimolar proportions of two branched peptide sequences bis(FLIVI)-K-KKKK and bis(FLIVIGSII)-K-KKKK that self-assemble to form bilayer delimited capsules. In two recent publications we described the lipid analogous characteristics of our BAPCs, examined their initial assembly, mode of fusion, solute encapsulation, and resizing and delineated their capability to be maintained at a specific size by storing them at 4 °C. In this report we describe the stability, size limitations of encapsulation, cellular localization, retention and, bio-distribution of the BAPCs in vivo. The ability of our constructs to retain alpha particle emitting radionuclides without any apparent leakage and their persistence in the peri-nuclear region of the cell for extended periods of time, coupled with their ease of preparation and potential tune-ability, makes them attractive as biocompatible carriers for targeted cancer therapy using particle emitting radioisotopes. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.
AB - Branched amphiphilic peptide capsules (BAPCs) are peptide nano-spheres comprised of equimolar proportions of two branched peptide sequences bis(FLIVI)-K-KKKK and bis(FLIVIGSII)-K-KKKK that self-assemble to form bilayer delimited capsules. In two recent publications we described the lipid analogous characteristics of our BAPCs, examined their initial assembly, mode of fusion, solute encapsulation, and resizing and delineated their capability to be maintained at a specific size by storing them at 4 °C. In this report we describe the stability, size limitations of encapsulation, cellular localization, retention and, bio-distribution of the BAPCs in vivo. The ability of our constructs to retain alpha particle emitting radionuclides without any apparent leakage and their persistence in the peri-nuclear region of the cell for extended periods of time, coupled with their ease of preparation and potential tune-ability, makes them attractive as biocompatible carriers for targeted cancer therapy using particle emitting radioisotopes. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.
KW - Alpha particle therapy
KW - BAPC
KW - Nano-capsule
KW - Peptide capsule
KW - Self-assembling peptide
UR - http://www.scopus.com/inward/record.url?scp=84903763113&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84903763113&partnerID=8YFLogxK
U2 - 10.1016/j.bbamem.2014.02.005
DO - 10.1016/j.bbamem.2014.02.005
M3 - Article
C2 - 24565797
AN - SCOPUS:84903763113
SN - 0005-2736
VL - 1838
SP - 2296
EP - 2305
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
IS - 9
ER -