ABSTRACT
The objective of our study was to compare length of stay and wound complications after hybrid robotic transversus abdominis release (hrTAR) vs. robotic transversus abdominis release (rTAR) Two cohorts of patients undergoing robotic (rTAR) and hybrid robotic (hrTAR) performed by two surgeons at a single institution were analyzed. Mean length of stay (LOS) and incidence of surgical site occurrences (SSO) were compared. 57 patients undergoing rTAR and 25 patients undergoing hrTAR were analyzed. The hrTAR group had larger mean hernia dimensions and a larger proportion of men but otherwise the patient cohorts were similar. LOS was not statistically different between rTAR and hrTAR (2.8 vs 3.7 days p = 0.06). We found no difference in incidence of surgical site occurrences between the two groups (7.0% vs 4.0% p = 0.52). Hybrid robotic assisted TAR allows for repair of complex ventral hernias with similar lengths of stay and wound morbidity to pure robotic repairs.
Subject(s)
Abdominal Muscles/surgery , Hernia, Ventral/surgery , Herniorrhaphy/methods , Length of Stay/statistics & numerical data , Robotic Surgical Procedures/methods , Surgical Wound Dehiscence/epidemiology , Surgical Wound Infection/epidemiology , Adult , Aged , Female , Humans , Incidence , Male , Middle Aged , Retrospective Studies , Treatment OutcomeABSTRACT
A fluorescently labeled 20-residue polyglutamic acid (polyE) peptide 20 amino acid length polyglutamic acid (E(20)) was used to study structural changes which occur in E(20) as it co-aggregates with other unlabeled polyE peptides. Resonance energy transfer (RET) was performed using an o-aminobenzamide donor at the N-terminus and 3-nitrotyrosine acceptor at the C-terminus of E(20). PolyE aggregates were not defined as amyloid, as they were nonfibrillar and did not bind congo red. Circular dichroism measurements indicate that polyE aggregation involves a transition from alpha-helical monomers to aggregated beta-sheets. Soluble oligomers are also produced along with aggregates in the reaction, as determined through size exclusion chromatography. Time-resolved and steady-state RET measurements reveal four dominant E(20) conformations: (1) a partially collapsed conformation (24 A donor-acceptor distance) in monomers, (2) an extended conformation in soluble oligomers (>29 A donor-acceptor distance), (3) a minor partially collapsed conformation (22 A donor-acceptor distance) in aggregates, and (4) a major highly collapsed conformation (13 A donor-acceptor distance) in aggregates. These findings demonstrate the use of RET as a means of determining angstrom-level structural details of soluble oligomer and aggregated states of proteins.
