NDLI: Functional Characterization of a Melittin Analog Containing a Non-natural Tryptophan Analog

Please wait, while we are loading the content...

Functional Characterization of a Melittin Analog Containing a Non-natural Tryptophan Analog

Content Provider	PubMed Central
Author	Ridgway, Zachary Picciano, Angela L. Gosavi, Pallavi M. Moroz, Yurii S. Angevine, Christopher E. Chavis, Amy E. Reiner, Joseph E. Korendovych, Ivan V. Caputo, Gregory A.
Abstract	Tryptophan (Trp) is a naturally occurring amino acid, which exhibits fluorescence emission properties that are dependent on the polarity of the local environment around the Trp side chain. However, this sensitivity also complicates interpretation of fluorescence emission data. A non-natural analogue of tryptophan, β-(1-azulenyl)-L-alanine, exhibits fluorescence insensitive to local solvent polarity and does not impact the structure or characteristics of several peptides examined. In this study we investigated the effect of replacing Trp with β-(1-azulenyl)-L-alanine in the well-known bee-venom peptide melittin. This peptide provides a model framework for investigating the impact of replacing Trp with β-(1-azulenyl)-L- alanine in a functional peptide system that undergoes significant shifts in Trp fluorescence emission upon binding to lipid bilayers. Microbiological methods including assessment of the antimicrobial activity by minimal inhibitory concentration (MIC) assays and bacterial membrane permeability assays indicated little difference between the Trp and the β-(1-azulenyl)-L-alanine-substituted versions of melittin. Circular dichroism spectroscopy showed both that peptides adopted the expected α-helical structures when bound to phospholipid bilayers and electrophysiological analysis indicated that both created membrane disruptions leading to significant conductance increases across model membranes. Both peptides exhibited a marked protection of the respective fluorophores when bound to bilayers indicating a similar membrane-bound topology. As expected, while fluorescence quenching and CD indicate the peptides are stably bound to lipid vesicles, the peptide containing β-(1-azulenyl)-L-alanine exhibited no fluorescence emission shift upon binding while the natural Trp exhibited >10 nm shift in emission spectrum barycenter. Taken together, the β-(1-azulenyl)-L-alanine can serve as a solvent insensitive alternative to Trp that does not have significant impacts on structure or function of membrane interacting peptides.
Related Links	http://dx.doi.org/10.1002/bip.22624
Ending Page	394
Page Count	11
Starting Page	384
File Format	PDF
ISSN	00063525
e-ISSN	10970282
Journal	Biopolymers
Issue Number	4
Volume Number	104
Language	English
Publisher Date	2015-07-01
Access Restriction	Open
Subject Keyword	Biophysics Organic Chemistry Biochemistry Biomaterials Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Medicine Biomaterials Biochemistry Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

4-Ketoproline: An Electrophilic Proline Analog for Bioconjugation

Characterization of a clinical polymer-drug conjugate using multiscale modeling

Biophysical Properties and Thermal Stability of Oligonucleotides of RNA Containing 7,8-Dihydro-8-hydroxyadenosine

Structural Characterization of the Regulatory Domain of Brain Carnitine Palmitoyltransferase 1

Structural and Electrostatic Characterization of Pariacoto Virus: Implications for Viral Asembly

Solid-Phase Synthesis, Characterization, and Cellular Activities of Collagen-Model Nanodiamond-Peptide Conjugates

A Novel and Simple Method of Production and Biophysical Characterization of a Mini-Membrane protein, Ost4p: A Subunit of Yeast Oligosaccharyl Transferase

Characterization of Secondary Amide Peptide Bonds Isomerization: Thermodynamics and Kinetics from 2D NMR Spectroscopy

Unraveling Cellulose Microfibrils: A Twisted Tale

Functional Characterization of a Melittin Analog Containing a Non-natural Tryptophan Analog

Similar Documents

4-Ketoproline: An Electrophilic Proline Analog for Bioconjugation

Characterization of a clinical polymer-drug conjugate using multiscale modeling

Biophysical Properties and Thermal Stability of Oligonucleotides of RNA Containing 7,8-Dihydro-8-hydroxyadenosine

Structural Characterization of the Regulatory Domain of Brain Carnitine Palmitoyltransferase 1

Structural and Electrostatic Characterization of Pariacoto Virus: Implications for Viral Asembly

Solid-Phase Synthesis, Characterization, and Cellular Activities of Collagen-Model Nanodiamond-Peptide Conjugates

A Novel and Simple Method of Production and Biophysical Characterization of a Mini-Membrane protein, Ost4p: A Subunit of Yeast Oligosaccharyl Transferase

Characterization of Secondary Amide Peptide Bonds Isomerization: Thermodynamics and Kinetics from 2D NMR Spectroscopy

Unraveling Cellulose Microfibrils: A Twisted Tale

Functional Characterization of a Melittin Analog Containing a Non-natural Tryptophan Analog