Albumin binding and hydrophobic character of promazine and chlorpromazine metabolites

1972 ◽  
Vol 272 (2) ◽  
pp. 121-130 ◽  
Author(s):  
J. Krieglstein ◽  
F. Lier ◽  
J. Michaelis
Keyword(s):  
Albumin Binding ◽  
Hydrophobic Character ◽  
Chlorpromazine Metabolites

scholarly journals Comparative Preclinical Evaluation of HER2-Targeting ABD-Fused Affibody® Molecules 177Lu-ABY-271 and 177Lu-ABY-027: Impact of DOTA Position on ABD Domain

Pharmaceutics ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 839
Author(s):  
Yongsheng Liu ◽  
Anzhelika Vorobyeva ◽  
Tianqi Xu ◽  
Anna Orlova ◽  
Annika Loftenius ◽  
...  
Keyword(s):  
A Priori ◽  
Albumin Binding ◽  
Tumor Uptake ◽  
Site Specific ◽  
Affibody Molecules ◽  
Preclinical Evaluation ◽  
Renal Uptake ◽  
C Terminus ◽  
Minimal Modification ◽  
Structure Properties

Radiolabeled Affibody-based targeting agent 177Lu-ABY-027, a fusion of an anti-HER2 Affibody molecule with albumin binding domain (ABD) site-specifically labeled at the C-terminus, has demonstrated a promising biodistribution profile in mice; binding of the construct to albumin prevents glomerular filtration and significantly reduces renal uptake. In this study, we tested the hypothesis that site-specific positioning of the chelator at helix 1 of ABD, at a maximum distance from the albumin binding site, would further increase the strength of binding to albumin and decrease the renal uptake. The new construct, ABY-271 with DOTA conjugated at the back of ABD, has been labelled with 177Lu. Targeting properties of 177Lu-ABY-271 and 177Lu-ABY-027 were compared directly. 177Lu-ABY-271 specifically accumulated in SKOV-3 xenografts in mice. The tumor uptake of 177Lu-ABY-271 exceeded uptake in any other organ 24 h and later after injection. However, the renal uptake of 177Lu-ABY-271 was two-fold higher than the uptake of 177Lu-ABY-027. Thus, the placement of chelator on helix 1 of ABD does not provide desirable reduction of renal uptake. To conclude, minimal modification of the design of Affibody molecules has a strong effect on biodistribution, which cannot be predicted a priori. This necessitates extensive structure-properties relationship studies to find an optimal design of Affibody-based targeting agents for therapy.

scholarly journals 18F labelled albumin binding synthons enabling PET imaging and enhanced target accumulation of biomolecules

2021 ◽  
Vol 96-97 ◽  
pp. S41-S42
Author(s):  
Andrew Hall ◽  
Alicia Corlett ◽  
Mohammad Haskali
Keyword(s):  
Pet Imaging ◽  
Albumin Binding

Adherence of platelets to in situ albumin-binding surfaces under flow conditions: role of surface-adsorbed albumin

2012 ◽  
Vol 7 (4) ◽  
pp. 045007 ◽  
Author(s):  
Sanjukta Guha Thakurta ◽  
Robert Miller ◽  
Anuradha Subramanian
Keyword(s):  
Albumin Binding ◽  
Flow Conditions

scholarly journals Novel albumin-binding photothermal agent ICG-IBA-RGD for targeted fluorescent imaging and photothermal therapy of cancer

RSC Advances ◽  
2021 ◽  
Vol 11 (13) ◽  
pp. 7226-7230
Author(s):  
Cheng Yu ◽  
Enhua Xiao ◽  
Pengfei Xu ◽  
Jingjing Lin ◽  
Linan Hu ◽  
...  
Keyword(s):  
Photothermal Therapy ◽  
Tumor Targeting ◽  
Fluorescent Imaging ◽  
Albumin Binding

In this work, we present a novel photothermal agent ICG-IBA-RGD based on albumin-binding strategy for enhanced tumor targeting imaging and photothermal therapy.

The serum albumin-binding region of streptococcal protein G: a bacterial fusion partner with carrier-related properties

1997 ◽  
Vol 201 (1) ◽  
pp. 115-123 ◽  
Author(s):  
Anders Sjölander ◽  
Per-Åke Nygren ◽  
Stefan Ståhl ◽  
Klavs Berzins ◽  
Mathias Uhlén ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Protein G ◽  
Albumin Binding ◽  
Fusion Partner ◽  
Binding Region ◽  
Streptococcal Protein G
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