Skip To Main Content
Barbara Pem on Muck Rack

Barbara Pem

As seen in: Wiley Online Library, MDPI, Taylor & Francis Online, Royal Society of Chemistry, BioRxiv
Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work. Claim your profile

Get in touch with Barbara

Contact Barbara, search articles and posts on X, monitor coverage, and track replies from one place.

Learn more about Muck Rack

Actions

Share this page

Is this you?

As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile

Articles

Peptide interaction with mixed lipid bilayers alters packing and hydrocarbon chain conformations

|
By Lea Pašalić, Barbara Pem, Andreja Jakas, Ana Čikoš
| Taylor & Francis Online
Abstract Cell-penetrating peptides (CPPs) with a cationic-hydrophobic character are recognized as carriers for delivering various therapeutics and diagnostic agents across cell membranes and into the cells. Among the most studied CPPs, nona-arginine (R9) exhibits superior penetration compared to its equally charged counterpart, nona-lysine (K9).
Open in Who Shared Issue with article?

UV Absorption Spectra of TAMRA and TAMRA Labeled Peptides: A Combined Density Functional Theory and Classical Molecular Dynamics Study

|
By Barbara Pem, Katarina Vazdar, Mercedes Kukulka, Lukasz Cwiklik
| Wiley Online Library Verified
1 Introduction Understanding the behavior of fluorescent probes at the molecular level is crucial for their effective application in biophysical research on model biological systems and living cells [1, 2]. 5-Carboxytetramethylrhodamine (TAMRA), a widely used fluorophore, plays a significant role in fluorescence imaging, molecular labeling, and biophysical assays due to its strong UV absorption and bright fluorescence emission [3].
Open in Who Shared Issue with article?

Peptide-induced hydration of lipid bilayers modulates packing pattern and conformations of hydrocarbon chains - a potential pathway for peptide translocation?

|
By Lea Pašalić, Barbara Pem, Andreja Jakas, Ana Čikoš
| BioRxiv
Abstract Cell-penetrating peptides (CPPs) with a cationic-hydrophobic character are recognized as carriers for delivering various therapeutics and diagnostic agents across cell membranes and into the cells. Among the most studied CPPs, nona-arginine (R9) exhibits superior penetration compared to nona-lysine (K9), suggesting that the penetration ability depends not only on charge, distribution and concentration of peptides but also on the lipid membrane composition.
Open in Who Shared Issue with article?
See all 7 articles