A Stroke Rehabilitation Educational Program for Occupational Therapy Students and Practitioners: Usability Study.

BACKGROUND: There are gaps in knowledge translation (KT) of current evidence-based practices regarding stroke assessment and rehabilitation delivered through teletherapy. A lack of this knowledge can prevent occupational therapy (OT) students and practitioners from implementing current research findings. OBJECTIVE: The aim of this pilot study was to create an educational program to translate knowledge into practice regarding the remote delivery of stroke assessment and rehabilitation to OT students and practitioners. Four areas of focus were addressed in the educational program, including KT, task-oriented training, stroke assessments, and telerehabilitation. METHODS: Two pilot studies were conducted to assess the knowledge gained via pretests and posttests of knowledge, followed by a System Usability Scale and general feedback questionnaire. Participants in study 1 were 5 OT practitioners and 1 OT assistant. Participants in study 2 were 9 current OT students. Four 1-hour modules were emailed weekly to participants over the course of 4 weeks, with each module covering a different topic (KT, task-oriented training, stroke assessments, and telerehabilitation). Preliminary results were reviewed using descriptive statistics. RESULTS: Statistically significant results were found with increased scores of knowledge for both students and practitioners. Most of the educational modules had an above-average score regarding value and positive feedback for the educational program as a whole from the participants. CONCLUSIONS: Overall, the results of this pilot study indicate that a web-based educational program is a valuable, informational method of increasing the translation of knowledge in the remote delivery of stroke assessment and rehabilitation. OT students and practitioners found the information presented to be valuable and relevant to their future profession and current practice.

The ergogenic effect of elastic therapeutic tape on stride and step length in fatigued runners.

OBJECTIVE: The purpose of this study was to determine if elastic therapeutic tape placed on anterior lower limbs would affect stride and step length in fatigued runners' gait. METHODS: Forty-two healthy participants were equally divided into a kinesiology tape group (Rocktape) and a no-tape control group. Participants in both groups underwent a baseline running gait test at 6 mph without tape. After this, participants engaged in an exhaustive lower body fatigue protocol until they reached maximal volitional exhaustion. Participants were then randomized to 1 of 2 interventions: (1) Experimental group, which had kinesiology tape placed under tension on the anterior aspect of their lower limbs bilaterally from the upper thigh to just below the patella, or (2) Control group, which did not receive taping. All participants then engaged in a similar 6-mph running gait postanalysis. Participant's gait was analyzed for 90 seconds during each test iteration. Researchers used a 2-way repeated-measures analysis of variance considering fatigue (prefatigue, postfatigue) and group (tape, no-tape) as subject factors. RESULTS: After the fatigue protocol, the no-tape group demonstrated a significant decrease in step length of 14.2 mm (P = .041) and stride length of 29.4 mm (P = .043). The kinesiology tape group did not demonstrate a significant decline in these gait parameters. CONCLUSIONS: In this preliminary study, placing elastic therapeutic tape over the anterior lower limbs demonstrated short-term preservation of runner step length and stride length in a fatigued state.

Embedding the Ni-SOD mimetic Ni-NCC within a polypeptide sequence alters the specificity of the reaction pathway.

The unique metal abstracting peptide asparagine-cysteine-cysteine (NCC) binds nickel in a square planar 2N:2S geometry and acts as a mimic of the enzyme nickel superoxide dismutase (Ni-SOD). The Ni-NCC tripeptide complex undergoes rapid, site-specific chiral inversion to dld-NCC in the presence of oxygen. Superoxide scavenging activity increases proportionally with the degree of chiral inversion. Characterization of the NCC sequence within longer peptides with absorption, circular dichroism (CD), and magnetic CD (MCD) spectroscopies and mass spectrometry (MS) shows that the geometry of metal coordination is maintained, though the electronic properties of the complex are varied to a small extent because of bis-amide, rather than amine/amide, coordination. In addition, both Ni-tripeptide and Ni-pentapeptide complexes have charges of -2. This study demonstrates that the chiral inversion chemistry does not occur when NCC is embedded in a longer polypeptide sequence. Nonetheless, the superoxide scavenging reactivity of the embedded Ni-NCC module is similar to that of the chirally inverted tripeptide complex, which is consistent with a minor change in the reduction potential for the Ni-pentapeptide complex. Together, this suggests that the charge of the complex could affect the SOD activity as much as a change in the primary coordination sphere. In Ni-NCC and other Ni-SOD mimics, changes in chirality, superoxide scavenging activity, and oxidation of the peptide itself all depend on the presence of dioxygen or its reduced derivatives (e.g., superoxide), and the extent to which each of these distinct reactions occurs is ruled by electronic and steric effects that emenate from the organization of ligands around the metal center.

Controlling the chiral inversion reaction of the metallopeptide Ni-asparagine-cysteine-cysteine with dioxygen.

Synthetically generated metallopeptides have the potential to serve a variety of roles in biotechnology applications, but the use of such systems is often hampered by the inability to control secondary reactions. We have previously reported that the Ni(II) complex of the tripeptide LLL-asparagine-cysteine-cysteine, LLL-Ni(II)-NCC, undergoes metal-facilitated chiral inversion to dld-Ni(II)-NCC, which increases the observed superoxide scavenging activity. However, the mechanism for this process remained unexplored. Electronic absorption and circular dichroism studies of the chiral inversion reaction of Ni(II)-NCC reveal a unique dependence on dioxygen. Specifically, in the absence of dioxygen, the chiral inversion is not observed, even at elevated pH, whereas the addition of O(2) initiates this reactivity and concomitantly generates superoxide. Scavenging experiments using acetaldehyde are indicative of the formation of carbanion intermediates, demonstrating that inversion takes place by deprotonation of the alpha carbons of Asn1 and Cys3. Together, these data are consistent with the chiral inversion being dependent on the formation of a Ni(III)-NCC intermediate from Ni(II)-NCC and O(2). The data further suggest that the anionic thiolate and amide ligands in Ni(II)-NCC inhibit Cα-H deprotonation for the Ni(II) oxidation state, leading to a stable complex in the absence of O(2). Together, these results offer insights into the factors controlling reactivity in synthetic metallopeptides.

MAPping the chiral inversion and structural transformation of a metal-tripeptide complex having ni-superoxide dismutase activity.

The metal abstraction peptide (MAP) tag is a tripeptide sequence capable of abstracting a metal ion from a chelator and binding it with extremely high affinity at neutral pH. Initial studies on the nickel-bound form of the complex demonstrate that the tripeptide asparagine-cysteine-cysteine (NCC) binds metal with 2N:2S, square planar geometry and behaves as both a structural and functional mimic of Ni superoxide dismutase (Ni-SOD). Electronic absorption, circular dichroism (CD), and magnetic CD (MCD) data collected for Ni-NCC are consistent with a diamagnetic Ni(II) center. It is apparent from the CD signal of Ni-NCC that the optical activity of the complex changes over time. Mass spectrometry data show that the mass of the complex is unchanged. Combined with the CD data, this suggests that chiral rearrangement of the complex occurs. Following incubation of the nickel-containing peptide in D(2)O and back-exchange into H(2)O, incorporation of deuterium into non-exchangeable positions is observed, indicating chiral inversion occurs at two of the α carbon atoms in the peptide. Control peptides were used to further characterize the chirality of the final nickel-peptide complex, and density functional theory (DFT) calculations were performed to validate the hypothesized position of the chiral inversions. In total, these data indicate Ni-SOD activity is increased proportionally to the degree of structural change in the complex over time. Specifically, the relationship between the change in CD signal and change in SOD activity is linear.

Novel tripeptide model of nickel superoxide dismutase.

Nickel superoxide dismutase (Ni-SOD) catalyzes the disproportionation of superoxide to molecular oxygen and hydrogen peroxide, but the overall reaction mechanism has yet to be determined. Peptide-based models of the 2N:2S nickel coordination sphere of Ni-SOD have provided some insight into the mechanism of this enzyme. Here we show that the coordination sphere of Ni-SOD can be mimicked using the tripeptide asparagine-cysteine-cysteine (NCC). NCC binds nickel with extremely high affinity at physiological pH with 2N:2S geometry, as demonstrated by electronic absorption and circular dichroism (CD) data. Like Ni-SOD, Ni-NCC has mixed amine/amide ligation that favors metal-based oxidation over ligand-based oxidation. Electronic absorption, CD, and magnetic CD (MCD) data collected for Ni-NCC are consistent with a diamagnetic Ni(II) center bound in square-planar geometry. Ni-NCC is quasi-reversibly oxidized with a midpoint potential of 0.72(2) V (vs Ag/AgCl) and breaks down superoxide in an enzyme-based assay, supporting its potential use as a model for Ni-SOD chemistry.