2008
DOI: 10.1016/s0076-6879(08)01622-4
|View full text |Cite
|
Sign up to set email alerts
|

Chapter 22 Synthesis and Biophysical Characterization of Stabilized α‐Helices of BCL‐2 Domains

Abstract: Rational design of compounds to mimic the functional domains of BCL-2 family proteins requires chemical reproduction of the biologic complexity afforded by the relatively large and folded surfaces of BCL-2 homology (BH) domain peptide alpha-helices. Because the intermolecular handshakes of BCL-2 proteins are so critical to controlling cellular fate, we undertook the development of a toolbox of peptidic ligands that harness the natural potency and specificity of BH alpha-helices to interrogate and potentially m… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

2
110
0

Year Published

2010
2010
2022
2022

Publication Types

Select...
6
2
1

Relationship

4
5

Authors

Journals

citations
Cited by 90 publications
(112 citation statements)
references
References 38 publications
2
110
0
Order By: Relevance
“…SAHBs were synthesized, derivatized, purified, stored, reconstituted, and characterized by circular dichroism as described in detail previously (20,47). All peptides were purified by liquid chromatography/mass spectrometry to more than 95% purity and quantified by amino acid analysis.…”
Section: Methodsmentioning
confidence: 99%
“…SAHBs were synthesized, derivatized, purified, stored, reconstituted, and characterized by circular dichroism as described in detail previously (20,47). All peptides were purified by liquid chromatography/mass spectrometry to more than 95% purity and quantified by amino acid analysis.…”
Section: Methodsmentioning
confidence: 99%
“…Peptide synthesis, hydrocarbon stapling by olefin metathesis, and derivatization with FITC and biotin were performed according to our established methods (54,55). All peptides were purified by LC/MS to >95% purity and quantified by amino acid analysis.…”
Section: Methodsmentioning
confidence: 99%
“…Peptides were dissolved in 5 mM potassium phosphate (pH 7.5) to a final concentration of 50 μM. Precise concentrations were determined by amino acid analysis and used to calculate percent α-helical content as described previously (40).…”
Section: Methodsmentioning
confidence: 99%