Can BioSAXS detect ultrastructural changes of antifungal compounds in ?-an exploratory study.

The opportunistic yeast is the most common cause of candidiasis. With only four classes of antifungal drugs on the market, resistance is becoming a problem in the treatment of fungal infections, especially in immunocompromised patients. The development of novel antifungal drugs with different modes of action is urgent.

Rational Designed Hybrid Peptides Show up to a 6-Fold Increase in Antimicrobial Activity and Demonstrate Different Ultrastructural Changes as the Parental Peptides Measured by BioSAXS.

Antimicrobial peptides (AMPs) are a promising class of compounds being developed against multi-drug resistant bacteria. Hybridization has been reported to increase antimicrobial activity. Here, two proline-rich peptides (consP1: VRKPPYLPRPRPRPL-CONH and Bac5-v291: RWRRPIRRRPIRPPFWR-CONH) were combined with two arginine-isoleucine-rich peptides (optP1: KIILRIRWR-CONH and optP7: KRRVRWIIW-CONH).

BioSAXS Measurements Reveal That Two Antimicrobial Peptides Induce Similar Molecular Changes in Gram-Negative and Gram-Positive Bacteria.

Two highly active short broad-spectrum AMPs (14D and 69D) with unknown mode of action have been investigated in regards to their effect against the Gram-negative bacteria Escherichia and the Gram-positive bacteria methicillin-resistant (MRSA). Minimal inhibitory concentration (MIC) measurements using a cell density of 10 cfu/ml resulted in values between 16 and 32 µg/ml. Time-kill experiments using 10 cfu/ml revealed complete killing, except for 69D in combination with MRSA, where bacterial load was reduced a million times.