Single-session versus two-session placement of chest port and gastrostomy tube in patients with head and neck cancer: Is there any difference in the device-related early infection rates?

Background: It is unknown whether placement of a chest port (port) and a gastrostomy tube (G-tube) in a single session increases the risk of the early device infections in patients with head and neck cancer (HNC) undergoing chemoradiation.

Purpose: To compare the incidence of early (≤30 days) port and G-tube infections placed in a single session compared to two separate sessions in patients with HNC.

Material And Methods: Between January 2012 and December 2019, 169 patients with HNC undergoing chemoradiation had a port and a G-tube placed in a single session (single-session group), while 25 had both devices placed in two separate sessions (two-session group) within 30 days of each other.

Copper-binding anticancer peptides from the piscidin family: an expanded mechanism that encompasses physical and chemical bilayer disruption.

In the search for novel broad-spectrum therapeutics to fight chronic infections, inflammation, and cancer, host defense peptides (HDPs) have garnered increasing interest. Characterizing their biologically-active conformations and minimum motifs for function represents a requisite step to developing them into efficacious and safe therapeutics. Here, we demonstrate that metallating HDPs with Cu is an effective chemical strategy to improve their cytotoxicity on cancer cells.

Risk Factors for Early Port Infections in Adult Oncologic Patients.

Purpose: The purpose of this study was to retrospectively investigate risk factors for chest port (port) infections within 30 days of placement (early port infections) in adult oncologic patients.

Materials And Methods: This single-institution, three-center retrospective study identified 1,714 patients (868 males, 846 females; median age 60.0 years old) who underwent port placement between January 2013 and August 2017.

Complementary Effects of Host Defense Peptides Piscidin 1 and Piscidin 3 on DNA and Lipid Membranes: Biophysical Insights into Contrasting Biological Activities.

Piscidins were the first antimicrobial peptides discovered in the mast cells of vertebrates. While two family members, piscidin 1 (p1) and piscidin 3 (p3), have highly similar sequences and α-helical structures when bound to model membranes, p1 generally exhibits stronger antimicrobial and hemolytic activity than p3 for reasons that remain elusive. In this study, we combine activity assays and biophysical methods to investigate the mechanisms underlying the cellular function and differing biological potencies of these peptides, and report findings spanning three major facets.